The tumour suppressor OPCML promotes AXL inactivation by the phosphatase PTPRG in ovarian cancer

In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression can be mitigated by the expression of the GPI‐anchored tumour suppressor OPCML. Further, we demonstrate that AXL directly interacts with OPCML...

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Published inEMBO reports Vol. 19; no. 8
Main Authors Antony, Jane, Zanini, Elisa, Kelly, Zoe, Tan, Tuan Zea, Karali, Evdoxia, Alomary, Mohammad, Jung, Youngrock, Nixon, Katherine, Cunnea, Paula, Fotopoulou, Christina, Paterson, Andrew, Roy‐Nawathe, Sushmita, Mills, Gordon B, Huang, Ruby Yun‐Ju, Thiery, Jean Paul, Gabra, Hani, Recchi, Chiara
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.08.2018
Springer Nature B.V
John Wiley and Sons Inc
Subjects
Animals
AXL
Axl protein
Benzocycloheptenes - pharmacology
Cancer
Cell Adhesion Molecules - metabolism
Cell Line, Tumor
Cell migration
Cell Movement - drug effects
Cell Survival - drug effects
Chickens
Cholesterol
Cholesterol - metabolism
Coordination compounds
Deactivation
EMBO03
EMBO37
Enzyme Activation - drug effects
Epidermal growth factor receptors
Epithelial Cells - drug effects
Epithelial Cells - metabolism
Epithelial Cells - pathology
Fallopian Tubes - pathology
Female
Gene Silencing - drug effects
GPI-Linked Proteins - metabolism
Humans
Inactivation
Intercellular Signaling Peptides and Proteins - metabolism
Ligands
Lipids
MAP Kinase Signaling System - drug effects
Medical prognosis
Membrane Microdomains - metabolism
Motility
Neoplasm Invasiveness
OPCML
Ovarian cancer
Ovarian Neoplasms - metabolism
Ovarian Neoplasms - pathology
Phosphatase
Phosphorylation - drug effects
Protein Binding - drug effects
Proto-Oncogene Proteins - metabolism
PTPRG
Receptor Protein-Tyrosine Kinases - metabolism
Receptor-Like Protein Tyrosine Phosphatases, Class 5 - metabolism
Signaling
Suppressors
Treatment Outcome
Triazoles - pharmacology
Tumor Suppressor Proteins - metabolism
Tumors
AXL
ovarian cancer
OPCML
PTPRG
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Abstract In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression can be mitigated by the expression of the GPI‐anchored tumour suppressor OPCML. Further, we demonstrate that AXL directly interacts with OPCML, preferentially so when AXL is activated by its ligand Gas6. As a consequence, AXL accumulates in cholesterol‐rich lipid domains, where OPCML resides. Here, phospho‐AXL is brought in proximity to the lipid domain‐restricted phosphatase PTPRG, which de‐phosphorylates the RTK/ligand complex. This prevents AXL‐mediated transactivation of other RTKs (cMET and EGFR), thereby inhibiting sustained phospho‐ERK signalling, induction of the EMT transcription factor Slug, cell migration and invasion. From a translational perspective, we show that OPCML enhances the effect of the phase II AXL inhibitor R428 in vitro and in vivo . We therefore identify a novel mechanism by which two spatially restricted tumour suppressors, OPCML and PTPRG, coordinate to repress AXL‐dependent oncogenic signalling. Synopsis The GPI‐anchored tumour suppressor OPCML interacts with the oncogenic RTK AXL inducing its redistribution into cholesterol‐rich membrane domains. There, AXL is de‐phosphorylated by the resident phosphatase PTPRG, inhibiting AXL‐dependent signalling, motility and invasion. Binding of Gas6 to the oncogenic RTK AXL promotes its interaction with the tumour suppressor OPCML. The Gas6/AXL/OPCML complex accumulates in cholesterol‐rich lipid domains, where the phosphatase PTPRG de‐phosphorylates AXL. The coordinated action of OPCML and PTPRG blocks AXL signalling and inhibits Gas6‐stimulated motility and invasion in ovarian cancer cells. Graphical Abstract The GPI‐anchored tumour suppressor OPCML interacts with the oncogenic RTK AXL inducing its redistribution into cholesterol‐rich membrane domains. There, AXL is de‐phosphorylated by the resident phosphatase PTPRG, inhibiting AXL‐dependent signalling, motility and invasion.
AbstractList In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression can be mitigated by the expression of the GPI‐anchored tumour suppressor OPCML. Further, we demonstrate that AXL directly interacts with OPCML, preferentially so when AXL is activated by its ligand Gas6. As a consequence, AXL accumulates in cholesterol‐rich lipid domains, where OPCML resides. Here, phospho‐AXL is brought in proximity to the lipid domain‐restricted phosphatase PTPRG, which de‐phosphorylates the RTK/ligand complex. This prevents AXL‐mediated transactivation of other RTKs (cMET and EGFR), thereby inhibiting sustained phospho‐ERK signalling, induction of the EMT transcription factor Slug, cell migration and invasion. From a translational perspective, we show that OPCML enhances the effect of the phase II AXL inhibitor R428 in vitro and in vivo. We therefore identify a novel mechanism by which two spatially restricted tumour suppressors, OPCML and PTPRG, coordinate to repress AXL‐dependent oncogenic signalling. Synopsis The GPI‐anchored tumour suppressor OPCML interacts with the oncogenic RTK AXL inducing its redistribution into cholesterol‐rich membrane domains. There, AXL is de‐phosphorylated by the resident phosphatase PTPRG, inhibiting AXL‐dependent signalling, motility and invasion. Binding of Gas6 to the oncogenic RTK AXL promotes its interaction with the tumour suppressor OPCML. The Gas6/AXL/OPCML complex accumulates in cholesterol‐rich lipid domains, where the phosphatase PTPRG de‐phosphorylates AXL. The coordinated action of OPCML and PTPRG blocks AXL signalling and inhibits Gas6‐stimulated motility and invasion in ovarian cancer cells. The GPI‐anchored tumour suppressor OPCML interacts with the oncogenic RTK AXL inducing its redistribution into cholesterol‐rich membrane domains. There, AXL is de‐phosphorylated by the resident phosphatase PTPRG, inhibiting AXL‐dependent signalling, motility and invasion.
In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression can be mitigated by the expression of the GPI‐anchored tumour suppressor OPCML. Further, we demonstrate that AXL directly interacts with OPCML, preferentially so when AXL is activated by its ligand Gas6. As a consequence, AXL accumulates in cholesterol‐rich lipid domains, where OPCML resides. Here, phospho‐AXL is brought in proximity to the lipid domain‐restricted phosphatase PTPRG, which de‐phosphorylates the RTK/ligand complex. This prevents AXL‐mediated transactivation of other RTKs (cMET and EGFR), thereby inhibiting sustained phospho‐ERK signalling, induction of the EMT transcription factor Slug, cell migration and invasion. From a translational perspective, we show that OPCML enhances the effect of the phase II AXL inhibitor R428 in vitro and in vivo. We therefore identify a novel mechanism by which two spatially restricted tumour suppressors, OPCML and PTPRG, coordinate to repress AXL‐dependent oncogenic signalling.
In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression can be mitigated by the expression of the GPI-anchored tumour suppressor OPCML Further, we demonstrate that AXL directly interacts with OPCML, preferentially so when AXL is activated by its ligand Gas6. As a consequence, AXL accumulates in cholesterol-rich lipid domains, where OPCML resides. Here, phospho-AXL is brought in proximity to the lipid domain-restricted phosphatase PTPRG, which de-phosphorylates the RTK/ligand complex. This prevents AXL-mediated transactivation of other RTKs (cMET and EGFR), thereby inhibiting sustained phospho-ERK signalling, induction of the EMT transcription factor Slug, cell migration and invasion. From a translational perspective, we show that OPCML enhances the effect of the phase II AXL inhibitor R428 in vitro and in vivo We therefore identify a novel mechanism by which two spatially restricted tumour suppressors, OPCML and PTPRG, coordinate to repress AXL-dependent oncogenic signalling.In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression can be mitigated by the expression of the GPI-anchored tumour suppressor OPCML Further, we demonstrate that AXL directly interacts with OPCML, preferentially so when AXL is activated by its ligand Gas6. As a consequence, AXL accumulates in cholesterol-rich lipid domains, where OPCML resides. Here, phospho-AXL is brought in proximity to the lipid domain-restricted phosphatase PTPRG, which de-phosphorylates the RTK/ligand complex. This prevents AXL-mediated transactivation of other RTKs (cMET and EGFR), thereby inhibiting sustained phospho-ERK signalling, induction of the EMT transcription factor Slug, cell migration and invasion. From a translational perspective, we show that OPCML enhances the effect of the phase II AXL inhibitor R428 in vitro and in vivo We therefore identify a novel mechanism by which two spatially restricted tumour suppressors, OPCML and PTPRG, coordinate to repress AXL-dependent oncogenic signalling.
In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression can be mitigated by the expression of the GPI-anchored tumour suppressor OPCML Further, we demonstrate that AXL directly interacts with OPCML, preferentially so when AXL is activated by its ligand Gas6. As a consequence, AXL accumulates in cholesterol-rich lipid domains, where OPCML resides. Here, phospho-AXL is brought in proximity to the lipid domain-restricted phosphatase PTPRG, which de-phosphorylates the RTK/ligand complex. This prevents AXL-mediated transactivation of other RTKs (cMET and EGFR), thereby inhibiting sustained phospho-ERK signalling, induction of the EMT transcription factor Slug, cell migration and invasion. From a translational perspective, we show that OPCML enhances the effect of the phase II AXL inhibitor R428 and We therefore identify a novel mechanism by which two spatially restricted tumour suppressors, OPCML and PTPRG, coordinate to repress AXL-dependent oncogenic signalling.
In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression can be mitigated by the expression of the GPI‐anchored tumour suppressor OPCML. Further, we demonstrate that AXL directly interacts with OPCML, preferentially so when AXL is activated by its ligand Gas6. As a consequence, AXL accumulates in cholesterol‐rich lipid domains, where OPCML resides. Here, phospho‐AXL is brought in proximity to the lipid domain‐restricted phosphatase PTPRG, which de‐phosphorylates the RTK/ligand complex. This prevents AXL‐mediated transactivation of other RTKs (cMET and EGFR), thereby inhibiting sustained phospho‐ERK signalling, induction of the EMT transcription factor Slug, cell migration and invasion. From a translational perspective, we show that OPCML enhances the effect of the phase II AXL inhibitor R428 in vitro and in vivo . We therefore identify a novel mechanism by which two spatially restricted tumour suppressors, OPCML and PTPRG, coordinate to repress AXL‐dependent oncogenic signalling. Synopsis The GPI‐anchored tumour suppressor OPCML interacts with the oncogenic RTK AXL inducing its redistribution into cholesterol‐rich membrane domains. There, AXL is de‐phosphorylated by the resident phosphatase PTPRG, inhibiting AXL‐dependent signalling, motility and invasion. Binding of Gas6 to the oncogenic RTK AXL promotes its interaction with the tumour suppressor OPCML. The Gas6/AXL/OPCML complex accumulates in cholesterol‐rich lipid domains, where the phosphatase PTPRG de‐phosphorylates AXL. The coordinated action of OPCML and PTPRG blocks AXL signalling and inhibits Gas6‐stimulated motility and invasion in ovarian cancer cells. Graphical Abstract The GPI‐anchored tumour suppressor OPCML interacts with the oncogenic RTK AXL inducing its redistribution into cholesterol‐rich membrane domains. There, AXL is de‐phosphorylated by the resident phosphatase PTPRG, inhibiting AXL‐dependent signalling, motility and invasion.
In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression can be mitigated by the expression of the GPI ‐anchored tumour suppressor OPCML . Further, we demonstrate that AXL directly interacts with OPCML , preferentially so when AXL is activated by its ligand Gas6. As a consequence, AXL accumulates in cholesterol‐rich lipid domains, where OPCML resides. Here, phospho‐ AXL is brought in proximity to the lipid domain‐restricted phosphatase PTPRG , which de‐phosphorylates the RTK /ligand complex. This prevents AXL ‐mediated transactivation of other RTK s ( cMET and EGFR ), thereby inhibiting sustained phospho‐ ERK signalling, induction of the EMT transcription factor Slug, cell migration and invasion. From a translational perspective, we show that OPCML enhances the effect of the phase II AXL inhibitor R428 in vitro and in vivo . We therefore identify a novel mechanism by which two spatially restricted tumour suppressors, OPCML and PTPRG , coordinate to repress AXL ‐dependent oncogenic signalling.
Author Karali, Evdoxia
Alomary, Mohammad
Tan, Tuan Zea
Kelly, Zoe
Paterson, Andrew
Zanini, Elisa
Jung, Youngrock
Roy‐Nawathe, Sushmita
Nixon, Katherine
Huang, Ruby Yun‐Ju
Gabra, Hani
Thiery, Jean Paul
Antony, Jane
Cunnea, Paula
Recchi, Chiara
Fotopoulou, Christina
Mills, Gordon B
AuthorAffiliation 1 Department of Surgery and Cancer Ovarian Cancer Action Research Centre Imperial College London London UK
9 Present address: Institute for Stem Cell Biology and Regenerative Medicine Stanford CA USA
4 Division of Basic Science Research Department of Systems Biology The University of Texas MD Anderson Cancer Center Houston TX USA
5 Department of Obstetrics and Gynecology National University Health System Singapore Singapore
3 NUS Graduate School for Integrative Sciences and Engineering National University of Singapore Singapore Singapore
8 Early Clinical Development IMED Biotech Unit AstraZeneca Cambridge UK
6 Institute of Molecular and Cell Biology ASTAR (Agency for Science, Technology and Research) Singapore Singapore
2 Cancer Science Institute of Singapore National University of Singapore Singapore Singapore
7 Department of Biochemistry National University of Singapore Singapore Singapore
AuthorAffiliation_xml – name: 5 Department of Obstetrics and Gynecology National University Health System Singapore Singapore
– name: 9 Present address: Institute for Stem Cell Biology and Regenerative Medicine Stanford CA USA
– name: 6 Institute of Molecular and Cell Biology ASTAR (Agency for Science, Technology and Research) Singapore Singapore
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– name: 7 Department of Biochemistry National University of Singapore Singapore Singapore
– name: 1 Department of Surgery and Cancer Ovarian Cancer Action Research Centre Imperial College London London UK
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/29907679$$D View this record in MEDLINE/PubMed
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Cites_doi 10.1038/cdd.2014.157
10.1158/0008-5472.CAN-09-2997
10.1146/annurev.genet.41.110306.130146
10.1080/23723556.2016.1263716
10.1016/S0065-230X(08)00002-X
10.3322/caac.21208
10.1002/emmm.201201823
10.1158/0008-5472.CAN-10-1267
10.1038/nrc3847
10.1242/jcs.00812
10.1158/1535-7163.MCT-13-0170
10.1158/0008-5472.CAN-17-0392
10.18388/abp.2011_2212
10.18632/oncotarget.5983
10.4161/cc.9.13.12270
10.1016/j.canlet.2012.07.023
10.1016/j.devcel.2013.07.020
10.1126/scisignal.aai7619
10.1038/onc.2012.378
10.18632/oncotarget.5087
10.18632/oncotarget.3876
10.1038/nprot.2012.097
10.1371/journal.pone.0033183
10.1371/journal.pone.0094476
10.1038/35036052
10.1158/2159-8290.CD-11-0256
10.1038/nrc3447
10.1242/jcs.02950
10.1158/0008-5472.CAN-08-0904
10.1002/0471142956.cy1207s35
10.1016/j.devcel.2008.05.009
10.1158/1535-7163.MCT-17-0081
10.1038/ng.2330
10.1038/ng1183
10.1371/journal.pone.0002990
10.1242/jcs.02505
10.1016/0092-8674(95)90520-0
10.1126/scisignal.aaf8175
10.1042/bj3350433
10.1038/nrc1611
10.1126/scisignal.2004155
10.1177/28.2.6766487
10.1073/pnas.0509885103
10.1158/1535-7163.MCT-06-0334
10.1093/carcin/bgt372
10.1038/nature08987
10.4049/jimmunol.1401841
10.1016/S1535-6108(03)00162-4
10.1073/pnas.0530291100
10.1021/acs.jproteome.5b01035
10.1038/nrm1835
10.1016/j.ccell.2015.03.010
10.1038/nrc822
10.1038/42408
10.1016/j.bbrc.2013.03.082
10.1158/0008-5472.CAN-10-0258
10.1186/s12929-016-0229-4
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Issue 8
Keywords AXL
ovarian cancer
OPCML
PTPRG
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References Naora, Montell (CR2) 2005; 5
Mirenda, Toffali, Montresor, Scardoni, Sorio, Laudanna (CR51) 2015; 194
Siegel, Ma, Zou, Jemal (CR1) 2014; 64
Tan, Miow, Huang, Wong, Ye, Lau, Wu, Bin Abdul Hadi, Soong, Choolani (CR10) 2013; 5
Rea, Pinciroli, Sensi, Alciato, Bisaro, Lozneanu, Raspagliesi, Centritto, Cabodi, Defilippi (CR39) 2015; 6
Simons, Toomre (CR45) 2000; 1
Giles, Kalinowski, Candy, Epis, Zhang, Redfern, Stuart, Goodall, Leedman (CR53) 2013; 12
Meder, Moreno, Verkade, Vaz, Simons (CR57) 2006; 103
Langdon, Lawrie (CR55) 2001; 39
McKie, Vaughan, Zanini, Okon, Louis, de Sousa, Greene, Wang, Agarwal, Shaposhnikov (CR15) 2012; 2
Hauge, Frodin (CR24) 2006; 119
Halmos, Haura (CR4) 2016; 9
Elkabets, Pazarentzos, Juric, Sheng, Pelossof, Brook, Benzaken, Rodon, Morse, Yan (CR13) 2015; 27
Karst, Drapkin (CR32) 2012; 7
Shin, Blenis (CR26) 2010; 9
De Craene, Berx (CR20) 2013; 13
Bakiri, Macho‐Maschler, Custic, Niemiec, Guio‐Carrion, Hasenfuss, Eger, Muller, Beug, Wagner (CR30) 2015; 22
Yang, Weinberg (CR29) 2008; 14
Chua, Sim, Racine, Lee, Goh, Thiery (CR34) 2012; 7
Hudson, Anderson, Artez, Barker, Bell, Bernabe, Bhan, Calvo, Eerola (CR17) 2010; 464
Thiery, Sleeman (CR28) 2006; 7
Ozhan, Sezgin, Wehner, Pfister, Kuhl, Kagermeier‐Schenk, Kuhl, Schwille, Weidinger (CR43) 2013; 26
Ebisuya, Kondoh, Nishida (CR23) 2005; 118
Robinson, Karnovsky (CR36) 1980; 28
Zanini, Louis, Antony, Karali, Okon, McKie, Vaughan, El‐Bahrawy, Stebbing, Recchi (CR52) 2017; 16
Tibes, Qiu, Lu, Hennessy, Andreeff, Mills, Kornblau (CR58) 2006; 5
Brodsky, Fischer, Miller, Vang, MacLaughlan, Wu, Yu, Steinhoff, Collins, Smith (CR8) 2014; 9
Rankin, Fuh, Taylor, Krieg, Musser, Yuan, Wei, Kuo, Longacre, Giaccia (CR9) 2010; 70
Al‐Hajj, Wicha, Benito‐Hernandez, Morrison, Clarke (CR11) 2003; 100
Holland, Pan, Franci, Hu, Chang, Li, Duan, Torneros, Yu, Heckrodt (CR38) 2010; 70
Vial, Marshall (CR25) 2003; 116
Meyer, Miller, Gertler, Lauffenburger (CR22) 2013; 6
Sellar, Watt, Rabiasz, Stronach, Li, Miller, Massie, Miller, Contreras‐Moreira, Scott (CR14) 2003; 34
Vial, Sahai, Marshall (CR33) 2003; 4
Ilangumaran, Hoessli (CR35) 1998; 335
CR56
Della Peruta, Martinelli, Moratti, Pintani, Vezzalini, Mafficini, Grafone, Iacobucci, Soverini, Murineddu (CR46) 2010; 70
Lee, Lee, Kim (CR31) 2013; 434
Chen, Chen, Chen, Huang, Lin, Wu, Huang, Liu, Chang, Kao (CR44) 2016; 23
Antony, Huang (CR12) 2017; 77
Sys, Van Bockstal, Forsyth, Balke, Poffyn, Uyttendaele, Bracke, De Wever (CR59) 2012; 326
Lee, Jeng, Chen, Chung, Yuan (CR41) 2014; 35
Linger, Keating, Earp, Graham (CR6) 2008; 100
Cobaleda, Perez‐Caro, Vicente‐Duenas, Sanchez‐Garcia (CR19) 2007; 41
Thiery (CR27) 2002; 2
Stitt, Conn, Gore, Lai, Bruno, Radziejewski, Mattsson, Fisher, Gies, Jones (CR7) 1995; 80
Antony, Tan, Kelly, Low, Choolani, Recchi, Gabra, Thiery, Huang (CR3) 2016; 9
Shah, Inder, Shah, Cristino, McKie, Gabra, Davis, Hill (CR37) 2016; 15
Laczmanska, Sasiadek (CR47) 2011; 58
Tan, Yang, Ye, Low, Choolani, Tan, Thiery, Huang (CR18) 2015; 6
Zhang, Lee, Lin, Olivas, Au, LaFramboise, Abdel‐Rahman, Wang, Levine, Rho (CR54) 2012; 44
Cui, Ying, van Hasselt, Ng, Yu, Zhang, Jin, Liu, Rhim, Rha (CR16) 2008; 3
Cheung, Lung, Hung, Law, Cheng, Yau, Bangarusamy, Miller, Liu, Shao (CR48) 2008; 68
Graham, DeRyckere, Davies, Earp (CR5) 2014; 14
Gujral, Karp, Finski, Chan, Schwartz, MacBeath, Sorger (CR21) 2013; 32
Cheung, Ip, Chu, Cheng, Leong, Ko, Shuen, Lung, Lung (CR50) 2015; 6
Simons, Ikonen (CR42) 1997; 387
Shu, Sugimoto, Liu, Chang, Ye, Wang, Huang, Yan, Lin (CR49) 2010; 30
Huang, Antony, Tan, Tan (CR40) 2017; 4
2013; 26
2003; 116
2017; 4
2010; 464
2000; 1
2008; 3
2011; 58
2008; 100
2013; 5
2013; 6
2012; 326
2014; 64
2013; 13
2013; 12
2017; 77
2013; 434
1997; 387
2014; 14
2003; 4
2008; 68
2014; 9
2010; 70
2010; 30
2010; 9
1980; 28
2015; 6
2006; 119
2005; 118
2006; 7
2008; 14
2002; 2
2006; 5
2006
1998; 335
2016; 15
2003; 34
2015; 194
2012; 2
2015; 27
1995; 80
2013; 32
2017; 16
2015; 22
2005; 5
2014; 35
2001; 39
2007; 41
2012; 7
2012; 44
2003; 100
2016; 9
2016; 23
2006; 103
e_1_2_8_28_1
e_1_2_8_24_1
e_1_2_8_47_1
e_1_2_8_26_1
e_1_2_8_49_1
e_1_2_8_3_1
e_1_2_8_5_1
e_1_2_8_7_1
e_1_2_8_9_1
e_1_2_8_20_1
e_1_2_8_43_1
e_1_2_8_22_1
e_1_2_8_45_1
e_1_2_8_41_1
e_1_2_8_60_1
e_1_2_8_17_1
e_1_2_8_19_1
e_1_2_8_13_1
e_1_2_8_36_1
e_1_2_8_59_1
e_1_2_8_15_1
e_1_2_8_38_1
e_1_2_8_57_1
e_1_2_8_32_1
e_1_2_8_55_1
e_1_2_8_11_1
e_1_2_8_34_1
e_1_2_8_53_1
e_1_2_8_51_1
Shu ST (e_1_2_8_50_1) 2010; 30
e_1_2_8_30_1
e_1_2_8_29_1
e_1_2_8_25_1
e_1_2_8_46_1
e_1_2_8_27_1
e_1_2_8_48_1
e_1_2_8_2_1
e_1_2_8_4_1
e_1_2_8_6_1
e_1_2_8_8_1
e_1_2_8_21_1
e_1_2_8_42_1
e_1_2_8_23_1
e_1_2_8_44_1
e_1_2_8_40_1
Langdon SP (e_1_2_8_56_1) 2001; 39
e_1_2_8_18_1
e_1_2_8_39_1
e_1_2_8_14_1
e_1_2_8_35_1
e_1_2_8_16_1
e_1_2_8_37_1
e_1_2_8_58_1
e_1_2_8_10_1
e_1_2_8_31_1
e_1_2_8_12_1
e_1_2_8_33_1
e_1_2_8_54_1
e_1_2_8_52_1
29967225 - EMBO Rep. 2018 Aug;19(8)
References_xml – volume: 9
  start-page: ra97
  year: 2016
  ident: CR3
  article-title: The GAS6‐AXL signaling network is a mesenchymal (Mes) molecular subtype‐specific therapeutic target for ovarian cancer
  publication-title: Sci Signal
– volume: 6
  start-page: ra66
  year: 2013
  ident: CR22
  article-title: The receptor AXL diversifies EGFR signaling and limits the response to EGFR‐targeted inhibitors in triple‐negative breast cancer cells
  publication-title: Sci Signal
– volume: 35
  start-page: 769
  year: 2014
  end-page: 775
  ident: CR41
  article-title: Gas6/Axl pathway promotes tumor invasion through the transcriptional activation of Slug in hepatocellular carcinoma
  publication-title: Carcinogenesis
– volume: 9
  start-page: fs14
  year: 2016
  ident: CR4
  article-title: New twists in the AXL(e) of tumor progression
  publication-title: Sci Signal
– volume: 464
  start-page: 993
  year: 2010
  end-page: 998
  ident: CR17
  article-title: International network of cancer genome projects
  publication-title: Nature
– volume: 70
  start-page: 8896
  year: 2010
  end-page: 8906
  ident: CR46
  article-title: Protein tyrosine phosphatase receptor type gamma is a functional tumor suppressor gene specifically downregulated in chronic myeloid leukemia
  publication-title: Cancer Res
– volume: 7
  start-page: 131
  year: 2006
  end-page: 142
  ident: CR28
  article-title: Complex networks orchestrate epithelial‐mesenchymal transitions
  publication-title: Nat Rev Mol Cell Biol
– volume: 3
  start-page: e2990
  year: 2008
  ident: CR16
  article-title: OPCML is a broad tumor suppressor for multiple carcinomas and lymphomas with frequently epigenetic inactivation
  publication-title: PLoS One
– volume: 80
  start-page: 661
  year: 1995
  end-page: 670
  ident: CR7
  article-title: The anticoagulation factor protein S and its relative, Gas6, are ligands for the Tyro 3/Axl family of receptor tyrosine kinases
  publication-title: Cell
– volume: 26
  start-page: 331
  year: 2013
  end-page: 345
  ident: CR43
  article-title: Lypd6 enhances Wnt/beta‐catenin signaling by promoting Lrp6 phosphorylation in raft plasma membrane domains
  publication-title: Dev Cell
– volume: 14
  start-page: 818
  year: 2008
  end-page: 829
  ident: CR29
  article-title: Epithelial‐mesenchymal transition: at the crossroads of development and tumor metastasis
  publication-title: Dev Cell
– volume: 1
  start-page: 31
  year: 2000
  end-page: 39
  ident: CR45
  article-title: Lipid rafts and signal transduction
  publication-title: Nat Rev Mol Cell Biol
– volume: 7
  start-page: e33183
  year: 2012
  ident: CR34
  article-title: A cell‐based small molecule screening method for identifying inhibitors of epithelial‐mesenchymal transition in carcinoma
  publication-title: PLoS One
– volume: 12
  start-page: 2541
  year: 2013
  end-page: 2558
  ident: CR53
  article-title: Axl mediates acquired resistance of head and neck cancer cells to the epidermal growth factor receptor inhibitor erlotinib
  publication-title: Mol Cancer Ther
– volume: 77
  start-page: 3725
  year: 2017
  end-page: 3732
  ident: CR12
  article-title: AXL‐driven EMT state as a targetable conduit in cancer
  publication-title: Cancer Res
– volume: 32
  start-page: 3470
  year: 2013
  end-page: 3476
  ident: CR21
  article-title: Profiling phospho‐signaling networks in breast cancer using reverse‐phase protein arrays
  publication-title: Oncogene
– volume: 5
  start-page: 983
  year: 2013
  end-page: 998
  ident: CR10
  article-title: Functional genomics identifies five distinct molecular subtypes with clinical relevance and pathways for growth control in epithelial ovarian cancer
  publication-title: EMBO Mol Med
– volume: 70
  start-page: 7570
  year: 2010
  end-page: 7579
  ident: CR9
  article-title: AXL is an essential factor and therapeutic target for metastatic ovarian cancer
  publication-title: Can Res
– volume: 100
  start-page: 35
  year: 2008
  end-page: 83
  ident: CR6
  article-title: TAM receptor tyrosine kinases: biologic functions, signaling, and potential therapeutic targeting in human cancer
  publication-title: Adv Cancer Res
– volume: 9
  start-page: 2483
  year: 2010
  end-page: 2484
  ident: CR26
  article-title: ERK2/Fra1/ZEB pathway induces epithelial‐to‐mesenchymal transition
  publication-title: Cell Cycle
– volume: 64
  start-page: 9
  year: 2014
  end-page: 29
  ident: CR1
  article-title: Cancer statistics, 2014
  publication-title: CA Cancer J Clin
– volume: 27
  start-page: 533
  year: 2015
  end-page: 546
  ident: CR13
  article-title: AXL mediates resistance to PI3Kalpha inhibition by activating the EGFR/PKC/mTOR axis in head and neck and esophageal squamous cell carcinomas
  publication-title: Cancer Cell
– volume: 118
  start-page: 2997
  year: 2005
  end-page: 3002
  ident: CR23
  article-title: The duration, magnitude and compartmentalization of ERK MAP kinase activity: mechanisms for providing signaling specificity
  publication-title: J Cell Sci
– volume: 194
  start-page: 2168
  year: 2015
  end-page: 2179
  ident: CR51
  article-title: Protein tyrosine phosphatase receptor type gamma is a JAK phosphatase and negatively regulates leukocyte integrin activation
  publication-title: J Immunol
– volume: 15
  start-page: 3451
  year: 2016
  end-page: 3462
  ident: CR37
  article-title: Integrative analysis of subcellular quantitative proteomics studies reveals functional cytoskeleton membrane‐lipid raft interactions in cancer
  publication-title: J Proteome Res
– volume: 2
  start-page: 156
  year: 2012
  end-page: 171
  ident: CR15
  article-title: The OPCML tumor suppressor functions as a cell surface repressor‐adaptor, negatively regulating receptor tyrosine kinases in epithelial ovarian cancer
  publication-title: Cancer Discov
– volume: 4
  start-page: 67
  year: 2003
  end-page: 79
  ident: CR33
  article-title: ERK‐MAPK signaling coordinately regulates activity of Rac1 and RhoA for tumor cell motility
  publication-title: Cancer Cell
– volume: 387
  start-page: 569
  year: 1997
  end-page: 572
  ident: CR42
  article-title: Functional rafts in cell membranes
  publication-title: Nature
– volume: 34
  start-page: 337
  year: 2003
  end-page: 343
  ident: CR14
  article-title: OPCML at 11q25 is epigenetically inactivated and has tumor‐suppressor function in epithelial ovarian cancer
  publication-title: Nat Genet
– volume: 6
  start-page: 43843
  year: 2015
  end-page: 43852
  ident: CR18
  article-title: CSIOVDB: a microarray gene expression database of epithelial ovarian cancer subtype
  publication-title: Oncotarget
– volume: 335
  start-page: 433
  issue: Pt 2
  year: 1998
  end-page: 440
  ident: CR35
  article-title: Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane
  publication-title: Biochem J
– volume: 116
  start-page: 4957
  year: 2003
  end-page: 4963
  ident: CR25
  article-title: Elevated ERK‐MAP kinase activity protects the FOS family member FRA‐1 against proteasomal degradation in colon carcinoma cells
  publication-title: J Cell Sci
– volume: 23
  start-page: 30
  year: 2016
  ident: CR44
  article-title: Betulinic acid enhances TGF‐beta signaling by altering TGF‐beta receptors partitioning between lipid‐raft/caveolae and non‐caveolae membrane microdomains in mink lung epithelial cells
  publication-title: J Biomed Sci
– volume: 2
  start-page: 442
  year: 2002
  end-page: 454
  ident: CR27
  article-title: Epithelial‐mesenchymal transitions in tumour progression
  publication-title: Nat Rev Cancer
– volume: 22
  start-page: 336
  year: 2015
  end-page: 350
  ident: CR30
  article-title: Fra‐1/AP‐1 induces EMT in mammary epithelial cells by modulating Zeb1/2 and TGFbeta expression
  publication-title: Cell Death Differ
– volume: 28
  start-page: 161
  year: 1980
  end-page: 168
  ident: CR36
  article-title: Evaluation of the polyene antibiotic filipin as a cytochemical probe for membrane cholesterol
  publication-title: J Histochem Cytochem
– volume: 103
  start-page: 329
  year: 2006
  end-page: 334
  ident: CR57
  article-title: Phase coexistence and connectivity in the apical membrane of polarized epithelial cells
  publication-title: Proc Natl Acad Sci USA
– volume: 7
  start-page: 1755
  year: 2012
  end-page: 1764
  ident: CR32
  article-title: Primary culture and immortalization of human fallopian tube secretory epithelial cells
  publication-title: Nat Protoc
– volume: 14
  start-page: 769
  year: 2014
  end-page: 785
  ident: CR5
  article-title: The TAM family: phosphatidylserine sensing receptor tyrosine kinases gone awry in cancer
  publication-title: Nat Rev Cancer
– volume: 434
  start-page: 8
  year: 2013
  end-page: 14
  ident: CR31
  article-title: Gas6 induces cancer cell migration and epithelial–mesenchymal transition through upregulation of MAPK and Slug
  publication-title: Biochem Biophys Res Comm
– volume: 70
  start-page: 1544
  year: 2010
  end-page: 1554
  ident: CR38
  article-title: R428, a selective small molecule inhibitor of Axl kinase, blocks tumor spread and prolongs survival in models of metastatic breast cancer
  publication-title: Cancer Res
– volume: 16
  start-page: 2246
  year: 2017
  end-page: 2256
  ident: CR52
  article-title: The tumor‐suppressor protein OPCML potentiates anti‐EGFR‐ and anti‐HER2‐targeted therapy in HER2‐positive ovarian and breast cancer
  publication-title: Mol Cancer Ther
– volume: 44
  start-page: 852
  year: 2012
  end-page: 860
  ident: CR54
  article-title: Activation of the AXL kinase causes resistance to EGFR‐targeted therapy in lung cancer
  publication-title: Nat Genet
– ident: CR56
– volume: 30
  start-page: 1937
  year: 2010
  end-page: 1946
  ident: CR49
  article-title: Function and regulatory mechanisms of the candidate tumor suppressor receptor protein tyrosine phosphatase gamma (PTPRG) in breast cancer cells
  publication-title: Anticancer Res
– volume: 6
  start-page: 30859
  year: 2015
  end-page: 30875
  ident: CR39
  article-title: Novel Axl‐driven signaling pathway and molecular signature characterize high‐grade ovarian cancer patients with poor clinical outcome
  publication-title: Oncotarget
– volume: 5
  start-page: 355
  year: 2005
  end-page: 366
  ident: CR2
  article-title: Ovarian Cancer Metastasis: integrating insights from disparate model organisms
  publication-title: Nat Rev Cancer
– volume: 58
  start-page: 467
  year: 2011
  end-page: 470
  ident: CR47
  article-title: Tyrosine phosphatases as a superfamily of tumor suppressors in colorectal cancer
  publication-title: Acta Biochim Pol
– volume: 6
  start-page: 13434
  year: 2015
  end-page: 13447
  ident: CR50
  article-title: PTPRG suppresses tumor growth and invasion via inhibition of Akt signaling in nasopharyngeal carcinoma
  publication-title: Oncotarget
– volume: 5
  start-page: 2512
  year: 2006
  end-page: 2521
  ident: CR58
  article-title: Reverse phase protein array: validation of a novel proteomic technology and utility for analysis of primary leukemia specimens and hematopoietic stem cells
  publication-title: Mol Cancer Ther
– volume: 326
  start-page: 69
  year: 2012
  end-page: 78
  ident: CR59
  article-title: Tumor grafts derived from sarcoma patients retain tumor morphology, viability, and invasion potential and indicate disease outcomes in the chick chorioallantoic membrane model
  publication-title: Cancer Lett
– volume: 4
  start-page: e1263716
  year: 2017
  ident: CR40
  article-title: Targeting the AXL signaling pathway in ovarian cancer
  publication-title: Mol Cell Oncol
– volume: 68
  start-page: 8137
  year: 2008
  end-page: 8145
  ident: CR48
  article-title: Functional analysis of a cell cycle‐associated, tumor‐suppressive gene, protein tyrosine phosphatase receptor type G, in nasopharyngeal carcinoma
  publication-title: Cancer Res
– volume: 9
  start-page: e94476
  year: 2014
  ident: CR8
  article-title: Expression profiling of primary and metastatic ovarian tumors reveals differences indicative of aggressive disease
  publication-title: PLoS One
– volume: 39
  start-page: 155
  year: 2001
  end-page: 159
  ident: CR55
  article-title: Establishment of ovarian cancer cell lines
  publication-title: Methods Mol Med
– volume: 100
  start-page: 3983
  year: 2003
  end-page: 3988
  ident: CR11
  article-title: Prospective identification of tumorigenic breast cancer cells
  publication-title: Proc Natl Acad Sci USA
– volume: 119
  start-page: 3021
  year: 2006
  end-page: 3023
  ident: CR24
  article-title: RSK and MSK in MAP kinase signalling
  publication-title: J Cell Sci
– volume: 41
  start-page: 41
  year: 2007
  end-page: 61
  ident: CR19
  article-title: Function of the zinc‐finger transcription factor SNAI2 in cancer and development
  publication-title: Annu Rev Genet
– volume: 13
  start-page: 97
  year: 2013
  end-page: 110
  ident: CR20
  article-title: Regulatory networks defining EMT during cancer initiation and progression
  publication-title: Nat Rev Cancer
– volume: 32
  start-page: 3470
  year: 2013
  end-page: 3476
  article-title: Profiling phospho‐signaling networks in breast cancer using reverse‐phase protein arrays
  publication-title: Oncogene
– volume: 4
  start-page: e1263716
  year: 2017
  article-title: Targeting the AXL signaling pathway in ovarian cancer
  publication-title: Mol Cell Oncol
– volume: 12
  start-page: 2541
  year: 2013
  end-page: 2558
  article-title: Axl mediates acquired resistance of head and neck cancer cells to the epidermal growth factor receptor inhibitor erlotinib
  publication-title: Mol Cancer Ther
– volume: 387
  start-page: 569
  year: 1997
  end-page: 572
  article-title: Functional rafts in cell membranes
  publication-title: Nature
– volume: 26
  start-page: 331
  year: 2013
  end-page: 345
  article-title: Lypd6 enhances Wnt/beta‐catenin signaling by promoting Lrp6 phosphorylation in raft plasma membrane domains
  publication-title: Dev Cell
– volume: 80
  start-page: 661
  year: 1995
  end-page: 670
  article-title: The anticoagulation factor protein S and its relative, Gas6, are ligands for the Tyro 3/Axl family of receptor tyrosine kinases
  publication-title: Cell
– volume: 41
  start-page: 41
  year: 2007
  end-page: 61
  article-title: Function of the zinc‐finger transcription factor SNAI2 in cancer and development
  publication-title: Annu Rev Genet
– volume: 9
  start-page: fs14
  year: 2016
  article-title: New twists in the AXL(e) of tumor progression
  publication-title: Sci Signal
– volume: 7
  start-page: 131
  year: 2006
  end-page: 142
  article-title: Complex networks orchestrate epithelial‐mesenchymal transitions
  publication-title: Nat Rev Mol Cell Biol
– volume: 434
  start-page: 8
  year: 2013
  end-page: 14
  article-title: Gas6 induces cancer cell migration and epithelial–mesenchymal transition through upregulation of MAPK and Slug
  publication-title: Biochem Biophys Res Comm
– volume: 5
  start-page: 983
  year: 2013
  end-page: 998
  article-title: Functional genomics identifies five distinct molecular subtypes with clinical relevance and pathways for growth control in epithelial ovarian cancer
  publication-title: EMBO Mol Med
– volume: 14
  start-page: 818
  year: 2008
  end-page: 829
  article-title: Epithelial‐mesenchymal transition: at the crossroads of development and tumor metastasis
  publication-title: Dev Cell
– volume: 70
  start-page: 8896
  year: 2010
  end-page: 8906
  article-title: Protein tyrosine phosphatase receptor type gamma is a functional tumor suppressor gene specifically downregulated in chronic myeloid leukemia
  publication-title: Cancer Res
– volume: 14
  start-page: 769
  year: 2014
  end-page: 785
  article-title: The TAM family: phosphatidylserine sensing receptor tyrosine kinases gone awry in cancer
  publication-title: Nat Rev Cancer
– volume: 103
  start-page: 329
  year: 2006
  end-page: 334
  article-title: Phase coexistence and connectivity in the apical membrane of polarized epithelial cells
  publication-title: Proc Natl Acad Sci USA
– volume: 70
  start-page: 1544
  year: 2010
  end-page: 1554
  article-title: R428, a selective small molecule inhibitor of Axl kinase, blocks tumor spread and prolongs survival in models of metastatic breast cancer
  publication-title: Cancer Res
– volume: 5
  start-page: 2512
  year: 2006
  end-page: 2521
  article-title: Reverse phase protein array: validation of a novel proteomic technology and utility for analysis of primary leukemia specimens and hematopoietic stem cells
  publication-title: Mol Cancer Ther
– volume: 119
  start-page: 3021
  year: 2006
  end-page: 3023
  article-title: RSK and MSK in MAP kinase signalling
  publication-title: J Cell Sci
– volume: 4
  start-page: 67
  year: 2003
  end-page: 79
  article-title: ERK‐MAPK signaling coordinately regulates activity of Rac1 and RhoA for tumor cell motility
  publication-title: Cancer Cell
– volume: 39
  start-page: 155
  year: 2001
  end-page: 159
  article-title: Establishment of ovarian cancer cell lines
  publication-title: Methods Mol Med
– volume: 9
  start-page: ra97
  year: 2016
  article-title: The GAS6‐AXL signaling network is a mesenchymal (Mes) molecular subtype‐specific therapeutic target for ovarian cancer
  publication-title: Sci Signal
– volume: 13
  start-page: 97
  year: 2013
  end-page: 110
  article-title: Regulatory networks defining EMT during cancer initiation and progression
  publication-title: Nat Rev Cancer
– volume: 64
  start-page: 9
  year: 2014
  end-page: 29
  article-title: Cancer statistics, 2014
  publication-title: CA Cancer J Clin
– volume: 116
  start-page: 4957
  year: 2003
  end-page: 4963
  article-title: Elevated ERK‐MAP kinase activity protects the FOS family member FRA‐1 against proteasomal degradation in colon carcinoma cells
  publication-title: J Cell Sci
– volume: 77
  start-page: 3725
  year: 2017
  end-page: 3732
  article-title: AXL‐driven EMT state as a targetable conduit in cancer
  publication-title: Cancer Res
– volume: 34
  start-page: 337
  year: 2003
  end-page: 343
  article-title: OPCML at 11q25 is epigenetically inactivated and has tumor‐suppressor function in epithelial ovarian cancer
  publication-title: Nat Genet
– volume: 30
  start-page: 1937
  year: 2010
  end-page: 1946
  article-title: Function and regulatory mechanisms of the candidate tumor suppressor receptor protein tyrosine phosphatase gamma (PTPRG) in breast cancer cells
  publication-title: Anticancer Res
– volume: 68
  start-page: 8137
  year: 2008
  end-page: 8145
  article-title: Functional analysis of a cell cycle‐associated, tumor‐suppressive gene, protein tyrosine phosphatase receptor type G, in nasopharyngeal carcinoma
  publication-title: Cancer Res
– volume: 9
  start-page: e94476
  year: 2014
  article-title: Expression profiling of primary and metastatic ovarian tumors reveals differences indicative of aggressive disease
  publication-title: PLoS One
– volume: 58
  start-page: 467
  year: 2011
  end-page: 470
  article-title: Tyrosine phosphatases as a superfamily of tumor suppressors in colorectal cancer
  publication-title: Acta Biochim Pol
– volume: 9
  start-page: 2483
  year: 2010
  end-page: 2484
  article-title: ERK2/Fra1/ZEB pathway induces epithelial‐to‐mesenchymal transition
  publication-title: Cell Cycle
– volume: 23
  start-page: 30
  year: 2016
  article-title: Betulinic acid enhances TGF‐beta signaling by altering TGF‐beta receptors partitioning between lipid‐raft/caveolae and non‐caveolae membrane microdomains in mink lung epithelial cells
  publication-title: J Biomed Sci
– volume: 16
  start-page: 2246
  year: 2017
  end-page: 2256
  article-title: The tumor‐suppressor protein OPCML potentiates anti‐EGFR‐ and anti‐HER2‐targeted therapy in HER2‐positive ovarian and breast cancer
  publication-title: Mol Cancer Ther
– volume: 70
  start-page: 7570
  year: 2010
  end-page: 7579
  article-title: AXL is an essential factor and therapeutic target for metastatic ovarian cancer
  publication-title: Can Res
– volume: 6
  start-page: ra66
  year: 2013
  article-title: The receptor AXL diversifies EGFR signaling and limits the response to EGFR‐targeted inhibitors in triple‐negative breast cancer cells
  publication-title: Sci Signal
– volume: 3
  start-page: e2990
  year: 2008
  article-title: OPCML is a broad tumor suppressor for multiple carcinomas and lymphomas with frequently epigenetic inactivation
  publication-title: PLoS One
– volume: 7
  start-page: e33183
  year: 2012
  article-title: A cell‐based small molecule screening method for identifying inhibitors of epithelial‐mesenchymal transition in carcinoma
  publication-title: PLoS One
– volume: 15
  start-page: 3451
  year: 2016
  end-page: 3462
  article-title: Integrative analysis of subcellular quantitative proteomics studies reveals functional cytoskeleton membrane‐lipid raft interactions in cancer
  publication-title: J Proteome Res
– volume: 28
  start-page: 161
  year: 1980
  end-page: 168
  article-title: Evaluation of the polyene antibiotic filipin as a cytochemical probe for membrane cholesterol
  publication-title: J Histochem Cytochem
– volume: 326
  start-page: 69
  year: 2012
  end-page: 78
  article-title: Tumor grafts derived from sarcoma patients retain tumor morphology, viability, and invasion potential and indicate disease outcomes in the chick chorioallantoic membrane model
  publication-title: Cancer Lett
– volume: 22
  start-page: 336
  year: 2015
  end-page: 350
  article-title: Fra‐1/AP‐1 induces EMT in mammary epithelial cells by modulating Zeb1/2 and TGFbeta expression
  publication-title: Cell Death Differ
– year: 2006
  article-title: Detecting protein‐protein interactions with CFP‐YFP FRET by acceptor photobleaching
  publication-title: Curr Protoc Cytom
– volume: 118
  start-page: 2997
  year: 2005
  end-page: 3002
  article-title: The duration, magnitude and compartmentalization of ERK MAP kinase activity: mechanisms for providing signaling specificity
  publication-title: J Cell Sci
– volume: 194
  start-page: 2168
  year: 2015
  end-page: 2179
  article-title: Protein tyrosine phosphatase receptor type gamma is a JAK phosphatase and negatively regulates leukocyte integrin activation
  publication-title: J Immunol
– volume: 35
  start-page: 769
  year: 2014
  end-page: 775
  article-title: Gas6/Axl pathway promotes tumor invasion through the transcriptional activation of Slug in hepatocellular carcinoma
  publication-title: Carcinogenesis
– volume: 27
  start-page: 533
  year: 2015
  end-page: 546
  article-title: AXL mediates resistance to PI3Kalpha inhibition by activating the EGFR/PKC/mTOR axis in head and neck and esophageal squamous cell carcinomas
  publication-title: Cancer Cell
– volume: 6
  start-page: 30859
  year: 2015
  end-page: 30875
  article-title: Novel Axl‐driven signaling pathway and molecular signature characterize high‐grade ovarian cancer patients with poor clinical outcome
  publication-title: Oncotarget
– volume: 7
  start-page: 1755
  year: 2012
  end-page: 1764
  article-title: Primary culture and immortalization of human fallopian tube secretory epithelial cells
  publication-title: Nat Protoc
– volume: 6
  start-page: 43843
  year: 2015
  end-page: 43852
  article-title: CSIOVDB: a microarray gene expression database of epithelial ovarian cancer subtype
  publication-title: Oncotarget
– volume: 44
  start-page: 852
  year: 2012
  end-page: 860
  article-title: Activation of the AXL kinase causes resistance to EGFR‐targeted therapy in lung cancer
  publication-title: Nat Genet
– volume: 5
  start-page: 355
  year: 2005
  end-page: 366
  article-title: Ovarian Cancer Metastasis: integrating insights from disparate model organisms
  publication-title: Nat Rev Cancer
– volume: 100
  start-page: 35
  year: 2008
  end-page: 83
  article-title: TAM receptor tyrosine kinases: biologic functions, signaling, and potential therapeutic targeting in human cancer
  publication-title: Adv Cancer Res
– volume: 1
  start-page: 31
  year: 2000
  end-page: 39
  article-title: Lipid rafts and signal transduction
  publication-title: Nat Rev Mol Cell Biol
– volume: 6
  start-page: 13434
  year: 2015
  end-page: 13447
  article-title: PTPRG suppresses tumor growth and invasion via inhibition of Akt signaling in nasopharyngeal carcinoma
  publication-title: Oncotarget
– volume: 335
  start-page: 433
  issue: Pt 2
  year: 1998
  end-page: 440
  article-title: Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane
  publication-title: Biochem J
– volume: 464
  start-page: 993
  year: 2010
  end-page: 998
  article-title: International network of cancer genome projects
  publication-title: Nature
– volume: 2
  start-page: 156
  year: 2012
  end-page: 171
  article-title: The OPCML tumor suppressor functions as a cell surface repressor‐adaptor, negatively regulating receptor tyrosine kinases in epithelial ovarian cancer
  publication-title: Cancer Discov
– volume: 2
  start-page: 442
  year: 2002
  end-page: 454
  article-title: Epithelial‐mesenchymal transitions in tumour progression
  publication-title: Nat Rev Cancer
– volume: 100
  start-page: 3983
  year: 2003
  end-page: 3988
  article-title: Prospective identification of tumorigenic breast cancer cells
  publication-title: Proc Natl Acad Sci USA
– ident: e_1_2_8_31_1
  doi: 10.1038/cdd.2014.157
– ident: e_1_2_8_39_1
  doi: 10.1158/0008-5472.CAN-09-2997
– ident: e_1_2_8_20_1
  doi: 10.1146/annurev.genet.41.110306.130146
– ident: e_1_2_8_41_1
  doi: 10.1080/23723556.2016.1263716
– ident: e_1_2_8_7_1
  doi: 10.1016/S0065-230X(08)00002-X
– ident: e_1_2_8_2_1
  doi: 10.3322/caac.21208
– ident: e_1_2_8_11_1
  doi: 10.1002/emmm.201201823
– ident: e_1_2_8_10_1
  doi: 10.1158/0008-5472.CAN-10-1267
– ident: e_1_2_8_6_1
  doi: 10.1038/nrc3847
– ident: e_1_2_8_26_1
  doi: 10.1242/jcs.00812
– ident: e_1_2_8_54_1
  doi: 10.1158/1535-7163.MCT-13-0170
– ident: e_1_2_8_13_1
  doi: 10.1158/0008-5472.CAN-17-0392
– ident: e_1_2_8_48_1
  doi: 10.18388/abp.2011_2212
– ident: e_1_2_8_19_1
  doi: 10.18632/oncotarget.5983
– ident: e_1_2_8_27_1
  doi: 10.4161/cc.9.13.12270
– ident: e_1_2_8_60_1
  doi: 10.1016/j.canlet.2012.07.023
– ident: e_1_2_8_44_1
  doi: 10.1016/j.devcel.2013.07.020
– ident: e_1_2_8_5_1
  doi: 10.1126/scisignal.aai7619
– ident: e_1_2_8_22_1
  doi: 10.1038/onc.2012.378
– ident: e_1_2_8_40_1
  doi: 10.18632/oncotarget.5087
– ident: e_1_2_8_51_1
  doi: 10.18632/oncotarget.3876
– ident: e_1_2_8_33_1
  doi: 10.1038/nprot.2012.097
– ident: e_1_2_8_35_1
  doi: 10.1371/journal.pone.0033183
– ident: e_1_2_8_9_1
  doi: 10.1371/journal.pone.0094476
– ident: e_1_2_8_46_1
  doi: 10.1038/35036052
– ident: e_1_2_8_16_1
  doi: 10.1158/2159-8290.CD-11-0256
– ident: e_1_2_8_21_1
  doi: 10.1038/nrc3447
– ident: e_1_2_8_25_1
  doi: 10.1242/jcs.02950
– ident: e_1_2_8_49_1
  doi: 10.1158/0008-5472.CAN-08-0904
– ident: e_1_2_8_57_1
  doi: 10.1002/0471142956.cy1207s35
– ident: e_1_2_8_30_1
  doi: 10.1016/j.devcel.2008.05.009
– ident: e_1_2_8_53_1
  doi: 10.1158/1535-7163.MCT-17-0081
– ident: e_1_2_8_55_1
  doi: 10.1038/ng.2330
– ident: e_1_2_8_15_1
  doi: 10.1038/ng1183
– ident: e_1_2_8_17_1
  doi: 10.1371/journal.pone.0002990
– ident: e_1_2_8_24_1
  doi: 10.1242/jcs.02505
– ident: e_1_2_8_8_1
  doi: 10.1016/0092-8674(95)90520-0
– ident: e_1_2_8_4_1
  doi: 10.1126/scisignal.aaf8175
– ident: e_1_2_8_36_1
  doi: 10.1042/bj3350433
– ident: e_1_2_8_3_1
  doi: 10.1038/nrc1611
– ident: e_1_2_8_23_1
  doi: 10.1126/scisignal.2004155
– ident: e_1_2_8_37_1
  doi: 10.1177/28.2.6766487
– volume: 30
  start-page: 1937
  year: 2010
  ident: e_1_2_8_50_1
  article-title: Function and regulatory mechanisms of the candidate tumor suppressor receptor protein tyrosine phosphatase gamma (PTPRG) in breast cancer cells
  publication-title: Anticancer Res
– ident: e_1_2_8_58_1
  doi: 10.1073/pnas.0509885103
– ident: e_1_2_8_59_1
  doi: 10.1158/1535-7163.MCT-06-0334
– ident: e_1_2_8_42_1
  doi: 10.1093/carcin/bgt372
– ident: e_1_2_8_18_1
  doi: 10.1038/nature08987
– ident: e_1_2_8_52_1
  doi: 10.4049/jimmunol.1401841
– ident: e_1_2_8_34_1
  doi: 10.1016/S1535-6108(03)00162-4
– volume: 39
  start-page: 155
  year: 2001
  ident: e_1_2_8_56_1
  article-title: Establishment of ovarian cancer cell lines
  publication-title: Methods Mol Med
– ident: e_1_2_8_12_1
  doi: 10.1073/pnas.0530291100
– ident: e_1_2_8_38_1
  doi: 10.1021/acs.jproteome.5b01035
– ident: e_1_2_8_29_1
  doi: 10.1038/nrm1835
– ident: e_1_2_8_14_1
  doi: 10.1016/j.ccell.2015.03.010
– ident: e_1_2_8_28_1
  doi: 10.1038/nrc822
– ident: e_1_2_8_43_1
  doi: 10.1038/42408
– ident: e_1_2_8_32_1
  doi: 10.1016/j.bbrc.2013.03.082
– ident: e_1_2_8_47_1
  doi: 10.1158/0008-5472.CAN-10-0258
– ident: e_1_2_8_45_1
  doi: 10.1186/s12929-016-0229-4
– reference: 29967225 - EMBO Rep. 2018 Aug;19(8):
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Snippet In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression...
In ovarian cancer, the prometastatic RTK AXL promotes motility, invasion and poor prognosis. Here, we show that reduced survival caused by AXL overexpression...
SourceID pubmedcentral
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pubmed
crossref
wiley
springer
SourceType Open Access Repository
Aggregation Database
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Enrichment Source
Publisher
SubjectTerms Animals
AXL
Axl protein
Benzocycloheptenes - pharmacology
Cancer
Cell Adhesion Molecules - metabolism
Cell Line, Tumor
Cell migration
Cell Movement - drug effects
Cell Survival - drug effects
Chickens
Cholesterol
Cholesterol - metabolism
Coordination compounds
Deactivation
EMBO03
EMBO37
Enzyme Activation - drug effects
Epidermal growth factor receptors
Epithelial Cells - drug effects
Epithelial Cells - metabolism
Epithelial Cells - pathology
Fallopian Tubes - pathology
Female
Gene Silencing - drug effects
GPI-Linked Proteins - metabolism
Humans
Inactivation
Intercellular Signaling Peptides and Proteins - metabolism
Ligands
Lipids
MAP Kinase Signaling System - drug effects
Medical prognosis
Membrane Microdomains - metabolism
Motility
Neoplasm Invasiveness
OPCML
Ovarian cancer
Ovarian Neoplasms - metabolism
Ovarian Neoplasms - pathology
Phosphatase
Phosphorylation - drug effects
Protein Binding - drug effects
Proto-Oncogene Proteins - metabolism
PTPRG
Receptor Protein-Tyrosine Kinases - metabolism
Receptor-Like Protein Tyrosine Phosphatases, Class 5 - metabolism
Signaling
Suppressors
Treatment Outcome
Triazoles - pharmacology
Tumor Suppressor Proteins - metabolism
Tumors
Title The tumour suppressor OPCML promotes AXL inactivation by the phosphatase PTPRG in ovarian cancer
URI https://link.springer.com/article/10.15252/embr.201745670
https://onlinelibrary.wiley.com/doi/abs/10.15252%2Fembr.201745670
https://www.ncbi.nlm.nih.gov/pubmed/29907679
https://www.proquest.com/docview/2081996092
https://www.proquest.com/docview/2056393859
https://pubmed.ncbi.nlm.nih.gov/PMC6073217
Volume 19
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