The Oncolytic Avian Reovirus p17 Protein Inhibits Invadopodia Formation in Murine Melanoma Cancer Cells by Suppressing the FAK/Src Pathway and the Formation of theTKs5/NCK1 Complex

To explore whether the p17 protein of oncolytic avian reovirus (ARV) mediates cell migration and invadopodia formation, we applied several molecular biological approaches for studying the involved cellular factors and signal pathways. We found that ARV p17 activates the p53/phosphatase and tensin ho...

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Published inViruses Vol. 16; no. 7; p. 1153
Main Authors Hsu, Chao-Yu, Li, Jyun-Yi, Yang, En-Ying, Liao, Tsai-Ling, Wen, Hsiao-Wei, Tsai, Pei-Chien, Ju, Tz-Chuen, Lye, Lon-Fye, Nielsen, Brent L., Liu, Hung-Jen
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 01.07.2024
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Abstract To explore whether the p17 protein of oncolytic avian reovirus (ARV) mediates cell migration and invadopodia formation, we applied several molecular biological approaches for studying the involved cellular factors and signal pathways. We found that ARV p17 activates the p53/phosphatase and tensin homolog (PTEN) pathway to suppress the focal adhesion kinase (FAK)/Src signaling and downstream signal molecules, thus inhibiting cell migration and the formation of invadopodia in murine melanoma cancer cell line (B16-F10). Importantly, p17-induced formation of invadopodia could be reversed in cells transfected with the mutant PTENC124A. p17 protein was found to significantly reduce the expression levels of tyrosine kinase substrate 5 (TKs5), Rab40b, non-catalytic region of tyrosine kinase adaptor protein 1 (NCK1), and matrix metalloproteinases (MMP9), suggesting that TKs5 and Rab40b were transcriptionally downregulated by p17. Furthermore, we found that p17 suppresses the formation of the TKs5/NCK1 complex. Coexpression of TKs5 and Rab40b in B16-F10 cancer cells reversed p17-modulated suppression of the formation of invadopodia. This work provides new insights into p17-modulated suppression of invadopodia formation by activating the p53/PTEN pathway, suppressing the FAK/Src pathway, and inhibiting the formation of the TKs5/NCK1 complex.
AbstractList To explore whether the p17 protein of oncolytic avian reovirus (ARV) mediates cell migration and invadopodia formation, we applied several molecular biological approaches for studying the involved cellular factors and signal pathways. We found that ARV p17 activates the p53/phosphatase and tensin homolog (PTEN) pathway to suppress the focal adhesion kinase (FAK)/Src signaling and downstream signal molecules, thus inhibiting cell migration and the formation of invadopodia in murine melanoma cancer cell line (B16-F10). Importantly, p17-induced formation of invadopodia could be reversed in cells transfected with the mutant PTEN . p17 protein was found to significantly reduce the expression levels of tyrosine kinase substrate 5 (TKs5), Rab40b, non-catalytic region of tyrosine kinase adaptor protein 1 (NCK1), and matrix metalloproteinases (MMP9), suggesting that TKs5 and Rab40b were transcriptionally downregulated by p17. Furthermore, we found that p17 suppresses the formation of the TKs5/NCK1 complex. Coexpression of TKs5 and Rab40b in B16-F10 cancer cells reversed p17-modulated suppression of the formation of invadopodia. This work provides new insights into p17-modulated suppression of invadopodia formation by activating the p53/PTEN pathway, suppressing the FAK/Src pathway, and inhibiting the formation of the TKs5/NCK1 complex.
To explore whether the p17 protein of oncolytic avian reovirus (ARV) mediates cell migration and invadopodia formation, we applied several molecular biological approaches for studying the involved cellular factors and signal pathways. We found that ARV p17 activates the p53/phosphatase and tensin homolog (PTEN) pathway to suppress the focal adhesion kinase (FAK)/Src signaling and downstream signal molecules, thus inhibiting cell migration and the formation of invadopodia in murine melanoma cancer cell line (B16-F10). Importantly, p17-induced formation of invadopodia could be reversed in cells transfected with the mutant PTEN[sub.C124A] . p17 protein was found to significantly reduce the expression levels of tyrosine kinase substrate 5 (TKs5), Rab40b, non-catalytic region of tyrosine kinase adaptor protein 1 (NCK1), and matrix metalloproteinases (MMP9), suggesting that TKs5 and Rab40b were transcriptionally downregulated by p17. Furthermore, we found that p17 suppresses the formation of the TKs5/NCK1 complex. Coexpression of TKs5 and Rab40b in B16-F10 cancer cells reversed p17-modulated suppression of the formation of invadopodia. This work provides new insights into p17-modulated suppression of invadopodia formation by activating the p53/PTEN pathway, suppressing the FAK/Src pathway, and inhibiting the formation of the TKs5/NCK1 complex.
To explore whether the p17 protein of oncolytic avian reovirus (ARV) mediates cell migration and invadopodia formation, we applied several molecular biological approaches for studying the involved cellular factors and signal pathways. We found that ARV p17 activates the p53/phosphatase and tensin homolog (PTEN) pathway to suppress the focal adhesion kinase (FAK)/Src signaling and downstream signal molecules, thus inhibiting cell migration and the formation of invadopodia in murine melanoma cancer cell line (B16-F10). Importantly, p17-induced formation of invadopodia could be reversed in cells transfected with the mutant PTENC124A. p17 protein was found to significantly reduce the expression levels of tyrosine kinase substrate 5 (TKs5), Rab40b, non-catalytic region of tyrosine kinase adaptor protein 1 (NCK1), and matrix metalloproteinases (MMP9), suggesting that TKs5 and Rab40b were transcriptionally downregulated by p17. Furthermore, we found that p17 suppresses the formation of the TKs5/NCK1 complex. Coexpression of TKs5 and Rab40b in B16-F10 cancer cells reversed p17-modulated suppression of the formation of invadopodia. This work provides new insights into p17-modulated suppression of invadopodia formation by activating the p53/PTEN pathway, suppressing the FAK/Src pathway, and inhibiting the formation of the TKs5/NCK1 complex.To explore whether the p17 protein of oncolytic avian reovirus (ARV) mediates cell migration and invadopodia formation, we applied several molecular biological approaches for studying the involved cellular factors and signal pathways. We found that ARV p17 activates the p53/phosphatase and tensin homolog (PTEN) pathway to suppress the focal adhesion kinase (FAK)/Src signaling and downstream signal molecules, thus inhibiting cell migration and the formation of invadopodia in murine melanoma cancer cell line (B16-F10). Importantly, p17-induced formation of invadopodia could be reversed in cells transfected with the mutant PTENC124A. p17 protein was found to significantly reduce the expression levels of tyrosine kinase substrate 5 (TKs5), Rab40b, non-catalytic region of tyrosine kinase adaptor protein 1 (NCK1), and matrix metalloproteinases (MMP9), suggesting that TKs5 and Rab40b were transcriptionally downregulated by p17. Furthermore, we found that p17 suppresses the formation of the TKs5/NCK1 complex. Coexpression of TKs5 and Rab40b in B16-F10 cancer cells reversed p17-modulated suppression of the formation of invadopodia. This work provides new insights into p17-modulated suppression of invadopodia formation by activating the p53/PTEN pathway, suppressing the FAK/Src pathway, and inhibiting the formation of the TKs5/NCK1 complex.
To explore whether the p17 protein of oncolytic avian reovirus (ARV) mediates cell migration and invadopodia formation, we applied several molecular biological approaches for studying the involved cellular factors and signal pathways. We found that ARV p17 activates the p53/phosphatase and tensin homolog (PTEN) pathway to suppress the focal adhesion kinase (FAK)/Src signaling and downstream signal molecules, thus inhibiting cell migration and the formation of invadopodia in murine melanoma cancer cell line (B16-F10). Importantly, p17-induced formation of invadopodia could be reversed in cells transfected with the mutant PTENC124A. p17 protein was found to significantly reduce the expression levels of tyrosine kinase substrate 5 (TKs5), Rab40b, non-catalytic region of tyrosine kinase adaptor protein 1 (NCK1), and matrix metalloproteinases (MMP9), suggesting that TKs5 and Rab40b were transcriptionally downregulated by p17. Furthermore, we found that p17 suppresses the formation of the TKs5/NCK1 complex. Coexpression of TKs5 and Rab40b in B16-F10 cancer cells reversed p17-modulated suppression of the formation of invadopodia. This work provides new insights into p17-modulated suppression of invadopodia formation by activating the p53/PTEN pathway, suppressing the FAK/Src pathway, and inhibiting the formation of the TKs5/NCK1 complex.
To explore whether the p17 protein of oncolytic avian reovirus (ARV) mediates cell migration and invadopodia formation, we applied several molecular biological approaches for studying the involved cellular factors and signal pathways. We found that ARV p17 activates the p53/phosphatase and tensin homolog (PTEN) pathway to suppress the focal adhesion kinase (FAK)/Src signaling and downstream signal molecules, thus inhibiting cell migration and the formation of invadopodia in murine melanoma cancer cell line (B16-F10). Importantly, p17-induced formation of invadopodia could be reversed in cells transfected with the mutant PTENC₁₂₄A. p17 protein was found to significantly reduce the expression levels of tyrosine kinase substrate 5 (TKs5), Rab40b, non-catalytic region of tyrosine kinase adaptor protein 1 (NCK1), and matrix metalloproteinases (MMP9), suggesting that TKs5 and Rab40b were transcriptionally downregulated by p17. Furthermore, we found that p17 suppresses the formation of the TKs5/NCK1 complex. Coexpression of TKs5 and Rab40b in B16-F10 cancer cells reversed p17-modulated suppression of the formation of invadopodia. This work provides new insights into p17-modulated suppression of invadopodia formation by activating the p53/PTEN pathway, suppressing the FAK/Src pathway, and inhibiting the formation of the TKs5/NCK1 complex.
Audience Academic
Author Liu, Hung-Jen
Ju, Tz-Chuen
Yang, En-Ying
Hsu, Chao-Yu
Wen, Hsiao-Wei
Nielsen, Brent L.
Liao, Tsai-Ling
Tsai, Pei-Chien
Lye, Lon-Fye
Li, Jyun-Yi
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CitedBy_id crossref_primary_10_3390_v17010099
Cites_doi 10.1038/nrc3792
10.1146/annurev-cellbio-092910-154216
10.1016/j.celrep.2014.07.050
10.3109/15419061.2014.923845
10.1016/j.cub.2013.08.044
10.1016/j.tcb.2017.03.003
10.1016/j.vetmic.2022.109545
10.3390/ijms21218117
10.1073/pnas.96.16.9021
10.1083/jcb.200801042
10.1074/jbc.274.29.20693
10.1034/j.1600-0625.2003.120201.x
10.1083/jcb.200407076
10.1038/nrm3141
10.1083/jcb.200812176
10.1023/A:1025819214508
10.2174/187152010794728657
10.1080/15384101.2015.1026523
10.1083/jcb.200212114
10.1101/sqb.2005.70.014
10.1083/jcb.201910132
10.1371/journal.pone.0133699
10.1371/journal.pone.0162356
10.1126/science.296.5573.1655
10.1016/j.ejcb.2008.02.008
10.3390/cells10020259
10.1016/j.virol.2003.12.004
10.1083/jcb.200809110
10.1242/jcs.046680
10.1074/jbc.RA118.002341
10.1016/j.ejcb.2008.01.008
10.18632/oncotarget.12954
10.1128/JVI.00851-19
10.1111/j.1749-6632.1998.tb10116.x
10.1242/jcs.193904
10.1128/jvi.00074-22
10.1016/j.biochi.2004.12.009
10.1016/j.ejcb.2005.10.004
10.3390/v9040090
10.1073/pnas.91.21.10148
10.1016/j.vetmic.2021.109277
10.1016/j.biochi.2005.01.013
10.21769/BioProtoc.997
10.1074/jbc.M112.390245
10.1016/j.ccr.2005.01.006
10.1126/scisignal.2002964
10.1091/mbc.e08-09-0949
10.3390/v15020523
10.1126/science.280.5369.1614
10.1177/1535370219861928
10.1083/jcb.201009126
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Keywords Rab40b
invadopodia
FAK/Src
p17
TKs5/NCK1 complex
MMP9
avian reoviruses
p53/PTEN
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References Seals (ref_48) 2005; 7
Cai (ref_16) 2019; 244
Murphy (ref_1) 2011; 12
Yamaguchi (ref_38) 2011; 193
Shih (ref_22) 2004; 321
Hsia (ref_43) 2003; 160
ref_19
Tamura (ref_35) 1999; 274
Tamura (ref_36) 1998; 280
ref_18
Linder (ref_55) 2011; 27
Eddy (ref_2) 2017; 27
Courtneidge (ref_5) 2005; 70
ref_25
Lochter (ref_13) 1998; 857
Fruman (ref_39) 1998; 67
ref_21
Oser (ref_56) 2009; 186
ref_20
Hoshino (ref_37) 2012; 5
Yamaguchi (ref_54) 2006; 85
Seano (ref_3) 2015; 14
Jacob (ref_8) 2013; 126
ref_29
ref_28
ref_26
Buschman (ref_46) 2009; 20
Clark (ref_42) 2008; 87
Yamaguchi (ref_53) 2005; 168
Dunn (ref_45) 2010; 10
Hofmann (ref_11) 2005; 87
Saykali (ref_34) 2014; 21
Gorden (ref_15) 2004; 23
Cantley (ref_40) 2002; 296
Chi (ref_23) 2013; 288
Chan (ref_33) 2009; 185
Jacob (ref_7) 2016; 129
Chiu (ref_17) 2018; 293
Stylli (ref_4) 2009; 122
Sulzmaier (ref_44) 2014; 14
Sharma (ref_6) 2013; 23
Huang (ref_27) 2022; 96
Schaller (ref_30) 1994; 14
Blouw (ref_50) 2008; 87
Bjorklund (ref_10) 2005; 1755
Chiu (ref_24) 2019; 93
Chen (ref_31) 1994; 91
ref_47
Mook (ref_14) 2004; 1705
Leong (ref_52) 2014; 8
Kahari (ref_9) 2005; 87
Oikawa (ref_41) 2008; 182
Iizuka (ref_51) 2016; 7
Kerkela (ref_12) 2003; 12
ref_49
Zhang (ref_32) 1999; 96
References_xml – volume: 14
  start-page: 598
  year: 2014
  ident: ref_44
  article-title: FAK in cancer: Mechanistic findings and clinical applications
  publication-title: Nat. Rev. Cancer
  doi: 10.1038/nrc3792
– volume: 27
  start-page: 185
  year: 2011
  ident: ref_55
  article-title: Degrading devices: Invadosomes in proteolytic cell invasion
  publication-title: Annu. Rev. Cell Dev. Biol.
  doi: 10.1146/annurev-cellbio-092910-154216
– volume: 8
  start-page: 1558
  year: 2014
  ident: ref_52
  article-title: Invadopodia are required for cancer cell extravasation and are a therapeutic target for metastasis
  publication-title: Cell Rep.
  doi: 10.1016/j.celrep.2014.07.050
– volume: 126
  start-page: 4647
  year: 2013
  ident: ref_8
  article-title: Rab40b regulates trafficking of MMP2 and MMP9 during invadopodia formation and invasion of breast cancer cells
  publication-title: J. Cell Sci.
– volume: 21
  start-page: 207
  year: 2014
  ident: ref_34
  article-title: Invadopodia, regulation, and assembly in cancer cell invasion
  publication-title: Cell Commun. Adhes.
  doi: 10.3109/15419061.2014.923845
– volume: 23
  start-page: 2079
  year: 2013
  ident: ref_6
  article-title: Tks5 and SHIP2 regulate invadopodium maturation, but not initiation, in breast carcinoma cells
  publication-title: Curr. Biol.
  doi: 10.1016/j.cub.2013.08.044
– volume: 27
  start-page: 595
  year: 2017
  ident: ref_2
  article-title: Tumor Cell Invado podia: Invasive Protrusions that Orchestrate Metastasis
  publication-title: Trends Cell Biol.
  doi: 10.1016/j.tcb.2017.03.003
– ident: ref_18
  doi: 10.1016/j.vetmic.2022.109545
– ident: ref_47
  doi: 10.3390/ijms21218117
– volume: 96
  start-page: 9021
  year: 1999
  ident: ref_32
  article-title: Focal adhesion kinase promotes phospholipase C-gamma1 activity
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.96.16.9021
– volume: 182
  start-page: 157
  year: 2008
  ident: ref_41
  article-title: Sequential signals toward podosome formation in NIH-src cells
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200801042
– volume: 274
  start-page: 20693
  year: 1999
  ident: ref_35
  article-title: PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.274.29.20693
– volume: 12
  start-page: 109
  year: 2003
  ident: ref_12
  article-title: Matrix metalloproteinases in tumor progression: Focus on basal and squamous cell skin cancer
  publication-title: Exp. Dermatol.
  doi: 10.1034/j.1600-0625.2003.120201.x
– volume: 168
  start-page: 441
  year: 2005
  ident: ref_53
  article-title: Molecular mechanisms of invadopodium formation: The role of the N-WASP-Arp2/3 complex pathway and cofilin
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200407076
– volume: 12
  start-page: 413
  year: 2011
  ident: ref_1
  article-title: The ‘ins’ and ‘outs’ of podosomes and invadopodia: Characteristics, formation and function
  publication-title: Nat. Rev. Mole. Cell Biol.
  doi: 10.1038/nrm3141
– volume: 186
  start-page: 571
  year: 2009
  ident: ref_56
  article-title: Cortactin regulates cofilin and N-WASp activities to control the stages of invadopodium assembly and maturation
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200812176
– volume: 1755
  start-page: 37
  year: 2005
  ident: ref_10
  article-title: Gelatinase-mediated migration and invasion of cancer cells
  publication-title: Biochim. Biophys. Acta
– volume: 23
  start-page: 119
  year: 2004
  ident: ref_15
  article-title: Matrix metalloproteinases in colorectal cancer: Is it worth talking about?
  publication-title: Cancer Metast. Rev.
  doi: 10.1023/A:1025819214508
– volume: 10
  start-page: 722
  year: 2010
  ident: ref_45
  article-title: Evolving therapies and FAK inhibitors for the treatment of cancer
  publication-title: Anticancer Agents Med. Chem.
  doi: 10.2174/187152010794728657
– volume: 14
  start-page: 1370
  year: 2015
  ident: ref_3
  article-title: Podosomes and invadopodia: Tools to breach vascular basement membrane
  publication-title: Cell Cycle
  doi: 10.1080/15384101.2015.1026523
– volume: 1705
  start-page: 69
  year: 2004
  ident: ref_14
  article-title: The role of gelatinases in colorectal cancer progression and metastasis
  publication-title: Biochim. Biophys. Acta
– volume: 160
  start-page: 753
  year: 2003
  ident: ref_43
  article-title: Differential regulation of cell motility and invasion by FAK
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200212114
– volume: 70
  start-page: 167
  year: 2005
  ident: ref_5
  article-title: The Src substrate Tks5, podosomes (invadopodia), and cancer cell invasion
  publication-title: Cold Spring Harb. Symp. Quant. Biol.
  doi: 10.1101/sqb.2005.70.014
– ident: ref_49
  doi: 10.1083/jcb.201910132
– volume: 14
  start-page: 1680
  year: 1994
  ident: ref_30
  article-title: Autophosphorylation of the focal adhesion kinase, pp125FAK, di rects SH2-dependent binding of pp60src
  publication-title: Mol. Cell. Biol.
– ident: ref_26
  doi: 10.1371/journal.pone.0133699
– ident: ref_25
  doi: 10.1371/journal.pone.0162356
– volume: 296
  start-page: 1655
  year: 2002
  ident: ref_40
  article-title: The phosphoinositide 3-kinase pathway
  publication-title: Science
  doi: 10.1126/science.296.5573.1655
– volume: 87
  start-page: 555
  year: 2008
  ident: ref_50
  article-title: A role for the podosome/invadopodia scaffold protein Tks5 in tumor growth in vivo
  publication-title: Eur. J. Cell Biol.
  doi: 10.1016/j.ejcb.2008.02.008
– ident: ref_21
  doi: 10.3390/cells10020259
– volume: 321
  start-page: 65
  year: 2004
  ident: ref_22
  article-title: Avian reovirus sigmaC protein induces apoptosis in cultured cells
  publication-title: Virology
  doi: 10.1016/j.virol.2003.12.004
– volume: 185
  start-page: 357
  year: 2009
  ident: ref_33
  article-title: FAK alters invadopodia and focal adhesion composition and dynamics to regulate breast cancer invasion
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.200809110
– volume: 122
  start-page: 2727
  year: 2009
  ident: ref_4
  article-title: Nck adaptor proteins link Tks5 to in va dopodia actin regulation and ECM degradation
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.046680
– volume: 293
  start-page: 12542
  year: 2018
  ident: ref_17
  article-title: Mechanistic insights into avian reovirus p17-modulated suppression of cell cycle CDK–cyclin complexes and enhancement of p53 and cyclin H interaction
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.RA118.002341
– volume: 87
  start-page: 581
  year: 2008
  ident: ref_42
  article-title: New role for cortactin in invadopodia: Regulation of protease secretion
  publication-title: Eur. J. Cell Biol.
  doi: 10.1016/j.ejcb.2008.01.008
– volume: 7
  start-page: 78473
  year: 2016
  ident: ref_51
  article-title: The role of Tks adaptor proteins in invadopodia formation, growth and metastasis of melanoma
  publication-title: Oncotarget
  doi: 10.18632/oncotarget.12954
– volume: 93
  start-page: e00851-19
  year: 2019
  ident: ref_24
  article-title: Heterogeneous nuclear ribonucleoprotein A1 and lamin A/C modulate nucleocytoplasmic shuttling of avian reovirus p17
  publication-title: J. Virol.
  doi: 10.1128/JVI.00851-19
– volume: 857
  start-page: 180
  year: 1998
  ident: ref_13
  article-title: The significance of matrix metalloproteinases during early stages of tumor progression
  publication-title: Ann. N. Y. Acad. Sci.
  doi: 10.1111/j.1749-6632.1998.tb10116.x
– volume: 129
  start-page: 4341
  year: 2016
  ident: ref_7
  article-title: The role and regulation of Rab40b–Tks5 complex during invadopodia formation and cancer cell invasion
  publication-title: J. Cell Sci.
  doi: 10.1242/jcs.193904
– volume: 96
  start-page: e00074-22
  year: 2022
  ident: ref_27
  article-title: p17-modulated Hsp90/Cdc37 complex governs avian reovirus replication by chaperoning p17, which promotes viral protein synthesis and accumulation of proteins σA and σC in viral factories
  publication-title: J. Virol.
  doi: 10.1128/jvi.00074-22
– volume: 67
  start-page: 481
  year: 1998
  ident: ref_39
  article-title: Phosphoinositide kinases
  publication-title: Annu. Rev. Bio Chem.
– volume: 87
  start-page: 273
  year: 2005
  ident: ref_9
  article-title: Collagenases in cancer
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2004.12.009
– volume: 85
  start-page: 213
  year: 2006
  ident: ref_54
  article-title: Invadopodia and podosomes in tumor invasion
  publication-title: Eur. J. Cell Biol.
  doi: 10.1016/j.ejcb.2005.10.004
– ident: ref_20
  doi: 10.3390/v9040090
– volume: 91
  start-page: 10148
  year: 1994
  ident: ref_31
  article-title: Association of focal adhesion kinase with its potential sub-strate phosphatidylinositol 3-kinase
  publication-title: Proc. Natl. Acad. Sci. USA
  doi: 10.1073/pnas.91.21.10148
– ident: ref_28
  doi: 10.1016/j.vetmic.2021.109277
– volume: 87
  start-page: 307
  year: 2005
  ident: ref_11
  article-title: Role of matrix metallopro teinases in melanoma cell invasion
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2005.01.013
– ident: ref_29
  doi: 10.21769/BioProtoc.997
– volume: 288
  start-page: 3571
  year: 2013
  ident: ref_23
  article-title: The p17 nonstructural protein of avian reovirus triggers autophagy enhancing virus replication via activation of phosphatase and tensin deleted on chromosome 10 (PTEN) and AMP activated protein kinase (AMPK), as well as dsRNA-dependent protein kinase (PKR)/eIF2a signaling pathways
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M112.390245
– volume: 7
  start-page: 155
  year: 2005
  ident: ref_48
  article-title: The adaptor protein Tks5/Fish is required for podosome formation and function, and for the protease-driven invasion of cancer cells
  publication-title: Cancer Cell
  doi: 10.1016/j.ccr.2005.01.006
– volume: 5
  start-page: ra66
  year: 2012
  ident: ref_37
  article-title: Network analysis of the focal adhesion to invadopodia transition identifies a PI3K-PKCa invasive signaling axis
  publication-title: Sci. Signal.
  doi: 10.1126/scisignal.2002964
– volume: 20
  start-page: 1302
  year: 2009
  ident: ref_46
  article-title: The novel adaptor protein Tks4 (SH3PXD2B) is required for functional podosome formation
  publication-title: Mol. Biol. Cell
  doi: 10.1091/mbc.e08-09-0949
– ident: ref_19
  doi: 10.3390/v15020523
– volume: 280
  start-page: 1614
  year: 1998
  ident: ref_36
  article-title: Inhibition of cell migration, spreading, andfocal adhesions by tumor suppressor PTEN
  publication-title: Science
  doi: 10.1126/science.280.5369.1614
– volume: 244
  start-page: 983
  year: 2019
  ident: ref_16
  article-title: The oncolytic efficacy and safety of avian reovirus and its dynamic distribution in infected mice
  publication-title: Exp. Biol. Med.
  doi: 10.1177/1535370219861928
– volume: 193
  start-page: 1275
  year: 2011
  ident: ref_38
  article-title: Phosphoinositide 3-kinase signaling pathway mediated by p110a regulates invadopodia formation
  publication-title: J. Cell Biol.
  doi: 10.1083/jcb.201009126
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Snippet To explore whether the p17 protein of oncolytic avian reovirus (ARV) mediates cell migration and invadopodia formation, we applied several molecular biological...
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SubjectTerms Adaptor proteins
Adaptor Proteins, Signal Transducing - genetics
Adaptor Proteins, Signal Transducing - metabolism
Angiogenesis
Animals
Antibodies
Avian orthoreovirus
avian reoviruses
Breast cancer
Cancer
Cancer cells
Cell adhesion & migration
Cell cycle
Cell Line, Tumor
cell lines
Cell migration
Cell Movement
Cellular signal transduction
Efficiency
FAK/Src
Focal adhesion kinase
Focal Adhesion Kinase 1 - genetics
Focal Adhesion Kinase 1 - metabolism
Gelatinase B
Genomes
Health aspects
Kinases
Matrix metalloproteinase
Medical research
Medicine, Experimental
Melanoma
Melanoma, Experimental - pathology
Melanoma, Experimental - therapy
metalloproteinases
Metastasis
Mice
mutants
neoplasm cells
non-specific protein-tyrosine kinase
Oncolysis
Oncolytic Viruses - genetics
Oncolytic Viruses - physiology
Orthoreovirus, Avian - genetics
Orthoreovirus, Avian - physiology
p17
p17 Protein
p53 Protein
p53/PTEN
Phosphotransferases
Physiological aspects
Plasmids
Podosomes - metabolism
Proteins
PTEN Phosphohydrolase - genetics
PTEN Phosphohydrolase - metabolism
PTEN protein
Rab40b
Reoviruses
Signal Transduction
Src protein
src-Family Kinases - genetics
src-Family Kinases - metabolism
TKs5/NCK1 complex
transcription (genetics)
Tumor Suppressor Protein p53 - genetics
Tumor Suppressor Protein p53 - metabolism
tyrosine
Viral proteins
Viral Proteins - genetics
Viral Proteins - metabolism
Wound healing
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Title The Oncolytic Avian Reovirus p17 Protein Inhibits Invadopodia Formation in Murine Melanoma Cancer Cells by Suppressing the FAK/Src Pathway and the Formation of theTKs5/NCK1 Complex
URI https://www.ncbi.nlm.nih.gov/pubmed/39066315
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Volume 16
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