Extracellular Phosphorylation of TIMP-2 by Secreted c-Src Tyrosine Kinase Controls MMP-2 Activity
The tissue inhibitor of metalloproteinases 2 (TIMP-2) is a specific endogenous inhibitor of matrix metalloproteinase 2 (MMP-2), which is a key enzyme that degrades the extracellular matrix and promotes tumor cell invasion. Although the TIMP-2:MMP-2 complex controls proteolysis, the signaling mechani...
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| Published in | iScience Vol. 1; pp. 87 - 96 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
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United States
Elsevier Inc
23.03.2018
Elsevier |
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| ISSN | 2589-0042 2589-0042 |
| DOI | 10.1016/j.isci.2018.02.004 |
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| Abstract | The tissue inhibitor of metalloproteinases 2 (TIMP-2) is a specific endogenous inhibitor of matrix metalloproteinase 2 (MMP-2), which is a key enzyme that degrades the extracellular matrix and promotes tumor cell invasion. Although the TIMP-2:MMP-2 complex controls proteolysis, the signaling mechanism by which the two proteins associate in the extracellular space remains unidentified. Here we report that TIMP-2 is phosphorylated outside the cell by secreted c-Src tyrosine kinase. As a consequence, phosphorylation at Y90 significantly enhances TIMP-2 potency as an MMP-2 inhibitor and weakens the catalytic action of the active enzyme. TIMP-2 phosphorylation also appears to be essential for its interaction with the latent enzyme proMMP-2 in vivo. Absence of the kinase or non-phosphorylatable Y90 abolishes TIMP-2 binding to the latent enzyme, ultimately hampering proMMP-2 activation. Together, TIMP-2 phosphorylation by secreted c-Src represents a critical extracellular regulatory mechanism that controls the proteolytic function of MMP-2.
[Display omitted]
•c-Src tyrosine kinase phosphorylates TIMP-2•Secreted c-Src phosphorylates TIMP-2 extracellularly•TIMP-2 Y90 phosphorylation promotes extracellular interaction with proMMP-2•Tyrosine phosphorylation of TIMP-2 regulates proMMP-2 processing and MMP-2 activity
Biochemistry; Enzymology; Molecular Biology |
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| AbstractList | The tissue inhibitor of metalloproteinases 2 (TIMP-2) is a specific endogenous inhibitor of matrix metalloproteinase 2 (MMP-2), which is a key enzyme that degrades the extracellular matrix and promotes tumor cell invasion. Although the TIMP-2:MMP-2 complex controls proteolysis, the signaling mechanism by which the two proteins associate in the extracellular space remains unidentified. Here we report that TIMP-2 is phosphorylated outside the cell by secreted c-Src tyrosine kinase. As a consequence, phosphorylation at Y90 significantly enhances TIMP-2 potency as an MMP-2 inhibitor and weakens the catalytic action of the active enzyme. TIMP-2 phosphorylation also appears to be essential for its interaction with the latent enzyme proMMP-2
in vivo
. Absence of the kinase or non-phosphorylatable Y90 abolishes TIMP-2 binding to the latent enzyme, ultimately hampering proMMP-2 activation. Together, TIMP-2 phosphorylation by secreted c-Src represents a critical extracellular regulatory mechanism that controls the proteolytic function of MMP-2.
•
c-Src tyrosine kinase phosphorylates TIMP-2
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Secreted c-Src phosphorylates TIMP-2 extracellularly
•
TIMP-2 Y90 phosphorylation promotes extracellular interaction with proMMP-2
•
Tyrosine phosphorylation of TIMP-2 regulates proMMP-2 processing and MMP-2 activity
Biochemistry; Enzymology; Molecular Biology The tissue inhibitor of metalloproteinases 2 (TIMP-2) is a specific endogenous inhibitor of matrix metalloproteinase 2 (MMP-2), which is a key enzyme that degrades the extracellular matrix and promotes tumor cell invasion. Although the TIMP-2:MMP-2 complex controls proteolysis, the signaling mechanism by which the two proteins associate in the extracellular space remains unidentified. Here we report that TIMP-2 is phosphorylated outside the cell by secreted c-Src tyrosine kinase. As a consequence, phosphorylation at Y90 significantly enhances TIMP-2 potency as an MMP-2 inhibitor and weakens the catalytic action of the active enzyme. TIMP-2 phosphorylation also appears to be essential for its interaction with the latent enzyme proMMP-2 in vivo. Absence of the kinase or non-phosphorylatable Y90 abolishes TIMP-2 binding to the latent enzyme, ultimately hampering proMMP-2 activation. Together, TIMP-2 phosphorylation by secreted c-Src represents a critical extracellular regulatory mechanism that controls the proteolytic function of MMP-2. [Display omitted] •c-Src tyrosine kinase phosphorylates TIMP-2•Secreted c-Src phosphorylates TIMP-2 extracellularly•TIMP-2 Y90 phosphorylation promotes extracellular interaction with proMMP-2•Tyrosine phosphorylation of TIMP-2 regulates proMMP-2 processing and MMP-2 activity Biochemistry; Enzymology; Molecular Biology The tissue inhibitor of metalloproteinases 2 (TIMP-2) is a specific endogenous inhibitor of matrix metalloproteinase 2 (MMP-2), which is a key enzyme that degrades the extracellular matrix and promotes tumor cell invasion. Although the TIMP-2:MMP-2 complex controls proteolysis, the signaling mechanism by which the two proteins associate in the extracellular space remains unidentified. Here we report that TIMP-2 is phosphorylated outside the cell by secreted c-Src tyrosine kinase. As a consequence, phosphorylation at Y90 significantly enhances TIMP-2 potency as an MMP-2 inhibitor and weakens the catalytic action of the active enzyme. TIMP-2 phosphorylation also appears to be essential for its interaction with the latent enzyme proMMP-2 in vivo. Absence of the kinase or non-phosphorylatable Y90 abolishes TIMP-2 binding to the latent enzyme, ultimately hampering proMMP-2 activation. Together, TIMP-2 phosphorylation by secreted c-Src represents a critical extracellular regulatory mechanism that controls the proteolytic function of MMP-2.The tissue inhibitor of metalloproteinases 2 (TIMP-2) is a specific endogenous inhibitor of matrix metalloproteinase 2 (MMP-2), which is a key enzyme that degrades the extracellular matrix and promotes tumor cell invasion. Although the TIMP-2:MMP-2 complex controls proteolysis, the signaling mechanism by which the two proteins associate in the extracellular space remains unidentified. Here we report that TIMP-2 is phosphorylated outside the cell by secreted c-Src tyrosine kinase. As a consequence, phosphorylation at Y90 significantly enhances TIMP-2 potency as an MMP-2 inhibitor and weakens the catalytic action of the active enzyme. TIMP-2 phosphorylation also appears to be essential for its interaction with the latent enzyme proMMP-2 in vivo. Absence of the kinase or non-phosphorylatable Y90 abolishes TIMP-2 binding to the latent enzyme, ultimately hampering proMMP-2 activation. Together, TIMP-2 phosphorylation by secreted c-Src represents a critical extracellular regulatory mechanism that controls the proteolytic function of MMP-2. The tissue inhibitor of metalloproteinases 2 (TIMP-2) is a specific endogenous inhibitor of matrix metalloproteinase 2 (MMP-2), which is a key enzyme that degrades the extracellular matrix and promotes tumor cell invasion. Although the TIMP-2:MMP-2 complex controls proteolysis, the signaling mechanism by which the two proteins associate in the extracellular space remains unidentified. Here we report that TIMP-2 is phosphorylated outside the cell by secreted c-Src tyrosine kinase. As a consequence, phosphorylation at Y90 significantly enhances TIMP-2 potency as an MMP-2 inhibitor and weakens the catalytic action of the active enzyme. TIMP-2 phosphorylation also appears to be essential for its interaction with the latent enzyme proMMP-2 in vivo. Absence of the kinase or non-phosphorylatable Y90 abolishes TIMP-2 binding to the latent enzyme, ultimately hampering proMMP-2 activation. Together, TIMP-2 phosphorylation by secreted c-Src represents a critical extracellular regulatory mechanism that controls the proteolytic function of MMP-2. The tissue inhibitor of metalloproteinases 2 (TIMP-2) is a specific endogenous inhibitor of matrix metalloproteinase 2 (MMP-2), which is a key enzyme that degrades the extracellular matrix and promotes tumor cell invasion. Although the TIMP-2:MMP-2 complex controls proteolysis, the signaling mechanism by which the two proteins associate in the extracellular space remains unidentified. Here we report that TIMP-2 is phosphorylated outside the cell by secreted c-Src tyrosine kinase. As a consequence, phosphorylation at Y90 significantly enhances TIMP-2 potency as an MMP-2 inhibitor and weakens the catalytic action of the active enzyme. TIMP-2 phosphorylation also appears to be essential for its interaction with the latent enzyme proMMP-2 in vivo. Absence of the kinase or non-phosphorylatable Y90 abolishes TIMP-2 binding to the latent enzyme, ultimately hampering proMMP-2 activation. Together, TIMP-2 phosphorylation by secreted c-Src represents a critical extracellular regulatory mechanism that controls the proteolytic function of MMP-2. : Biochemistry; Enzymology; Molecular Biology Subject Areas: Biochemistry, Enzymology, Molecular Biology |
| Author | Mollapour, Mehdi Bratslavsky, Gennady Bullard, Renee Stetler-Stevenson, William G. Bourboulia, Dimitra Woodford, Mark R. Sánchez-Pozo, Javier Baker-Williams, Alexander J. Wei, Beiyang |
| AuthorAffiliation | 1 Department of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA 3 Upstate Cancer Center, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA 4 Radiation Oncology Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA 2 Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA |
| AuthorAffiliation_xml | – name: 2 Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA – name: 4 Radiation Oncology Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA – name: 3 Upstate Cancer Center, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA – name: 1 Department of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA |
| Author_xml | – sequence: 1 givenname: Javier surname: Sánchez-Pozo fullname: Sánchez-Pozo, Javier organization: Department of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA – sequence: 2 givenname: Alexander J. surname: Baker-Williams fullname: Baker-Williams, Alexander J. organization: Department of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA – sequence: 3 givenname: Mark R. surname: Woodford fullname: Woodford, Mark R. organization: Department of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA – sequence: 4 givenname: Renee surname: Bullard fullname: Bullard, Renee organization: Department of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA – sequence: 5 givenname: Beiyang surname: Wei fullname: Wei, Beiyang organization: Radiation Oncology Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA – sequence: 6 givenname: Mehdi surname: Mollapour fullname: Mollapour, Mehdi organization: Department of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA – sequence: 7 givenname: William G. surname: Stetler-Stevenson fullname: Stetler-Stevenson, William G. organization: Radiation Oncology Branch, Center for Cancer Research, National Cancer Institute, 9000 Rockville Pike, Bethesda, MD 20892, USA – sequence: 8 givenname: Gennady surname: Bratslavsky fullname: Bratslavsky, Gennady organization: Department of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA – sequence: 9 givenname: Dimitra surname: Bourboulia fullname: Bourboulia, Dimitra email: bourmpod@upstate.edu organization: Department of Urology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, NY 13210, USA |
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| Cites_doi | 10.1038/nrc745 10.1038/ki.1993.27 10.1016/j.semcancer.2010.05.002 10.1074/jbc.273.2.871 10.1006/jmbi.1998.2223 10.1042/bj20030557 10.1016/j.cell.2010.03.015 10.1016/j.molcel.2010.01.005 10.1016/S0014-5793(03)01094-9 10.1002/jcb.25611 10.18632/oncotarget.1099 10.1074/jbc.M116.720250 10.1146/annurev.biochem.69.1.373 10.1016/S0968-0004(00)89103-3 10.1096/fj.06-7938com 10.1074/jbc.M101843200 10.1126/science.284.5420.1667 10.1186/gb-2011-12-11-233 10.1093/nar/gku1267 10.1101/cshperspect.a012872 10.1371/journal.pone.0093712 10.1074/jbc.M001270200 10.1371/journal.pone.0075836 10.1074/jbc.M108643200 10.1073/pnas.102185399 10.1074/jbc.M604423200 10.1074/jbc.270.10.5331 10.1074/jbc.M512009200 10.1074/jbc.M111.297069 10.1016/j.celrep.2015.07.004 10.1016/j.str.2011.09.021 10.1016/j.bbamcr.2010.01.003 10.1242/jcs.034843 10.1161/01.RES.0000070112.80711.3D 10.1515/bmc-2014-0003 10.1016/j.bbrc.2004.09.171 10.1074/jbc.274.30.21362 10.1371/journal.pone.0070811 10.1074/jbc.273.26.16098 10.1016/S0167-4889(96)00083-3 10.1074/jbc.M001271200 10.1074/jbc.272.47.29975 10.1021/bi00067a023 |
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| References | Visse, Nagase (bib38) 2003; 92 Lafleur, Tester, Thompson (bib20) 2003; 553 Morgunova, Tuuttila, Bergmann, Isupov, Lindqvist, Schneider, Tryggvason (bib22) 1999; 284 Sato, Obata, Kasahara, Nakayama, Fukumoto, Yamasaki, Yokoyama, Saito, Yamaguchi (bib33) 2009; 122 Brown, Kleiner, Unsworth, Stetler-Stevenson (bib8) 1993; 43 Di Noto, Paolini, Zendrini, Radeghieri, Caimi, Ricotta (bib12) 2013; 8 Wang, Juttermann, Soloway (bib39) 2000; 275 Strongin, Collier, Bannikov, Marmer, Grant, Goldberg (bib36) 1995; 270 Butler, Butler, Atkinson, Will, Tamura, Schade van Westrum, Crabbe, Clements, d'Ortho, Murphy (bib9) 1998; 273 Bourboulia, Stetler-Stevenson (bib6) 2010; 20 Kessenbrock, Plaks, Werb (bib18) 2010; 141 Morgunova, Tuuttila, Bergmann, Tryggvason (bib23) 2002; 99 Mollapour, Tsutsumi, Donnelly, Beebe, Tokita, Lee, Lee, Morra, Bourboulia, Scroggins (bib21) 2010; 37 Zou, Wu, Brew (bib44) 2016; 291 Willenbrock, Crabbe, Slocombe, Sutton, Docherty, Cockett, O'Shea, Brocklehurst, Phillips, Murphy (bib40) 1993; 32 DeRita, Zerlanko, Singh, Lu, Iozzo, Benovic, Languino (bib11) 2016; 118 Benham (bib3) 2012; 4 Kinoshita, Sato, Okada, Ohuchi, Imai, Okada, Seiki (bib19) 1998; 273 Sariahmetoglu, Crawford, Leon, Sawicka, Li, Ballermann, Holmes, Berthiaume, Holt, Sawicki (bib32) 2007; 21 Wingfield, Sax, Stahl, Kaufman, Palmer, Chung, Corcoran, Kleiner, Stetler-Stevenson (bib43) 1999; 274 Beebe, Mollapour, Scroggins, Prodromou, Xu, Tokita, Taldone, Pullen, Zierer, Lee (bib2) 2013; 4 Reinecke, Caplan (bib30) 2014; 5 Brew, Nagase (bib7) 2010; 1803 Olson, Gervasi, Mobashery, Fridman (bib27) 1997; 272 Batra, Soares, Mehner, Radisky (bib1) 2013; 8 Dunn, Woodford, Truman, Jensen, Schulman, Caza, Remillard, Loiselle, Wolfgeher, Blagg (bib13) 2015; 12 Tuuttila, Morgunova, Bergmann, Lindqvist, Maskos, Fernandez-Catalan, Bode, Tryggvason, Schneider (bib37) 1998; 284 Pinna, Ruzzene (bib28) 1996; 1314 Bernardo, Fridman (bib4) 2003; 374 Murphy (bib25) 2011; 12 Egeblad, Werb (bib14) 2002; 2 Rapti, Knauper, Murphy, Williamson (bib29) 2006; 281 English, Kassiri, Koskivirta, Atkinson, Di Grappa, Soloway, Nagase, Vuorio, Murphy, Khokha (bib15) 2006; 281 Morrison, Butler, Bigg, Roberts, Soloway, Overall (bib24) 2001; 276 Hornbeck, Zhang, Murray, Kornhauser, Latham, Skrzypek (bib16) 2015; 43 Nishi, Hashimoto, Panchenko (bib26) 2011; 19 Williamson, Hutton, Vogt, Rapti, Knauper, Carr, Murphy (bib42) 2001; 276 Roskoski (bib31) 2004; 324 Sharabi, Shirian, Grossman, Lebendiker, Sagi, Shifman (bib34) 2014; 9 Williams, Coppolino (bib41) 2011; 286 Songyang, Cantley (bib35) 1995; 20 Caterina, Yamada, Caterina, Longenecker, Holmback, Shi, Yermovsky, Engler, Birkedal-Hansen (bib10) 2000; 275 Hubbard, Till (bib17) 2000; 69 Betts, Russell (bib5) 2003 Roskoski (10.1016/j.isci.2018.02.004_bib31) 2004; 324 Morgunova (10.1016/j.isci.2018.02.004_bib23) 2002; 99 Hubbard (10.1016/j.isci.2018.02.004_bib17) 2000; 69 Reinecke (10.1016/j.isci.2018.02.004_bib30) 2014; 5 Williamson (10.1016/j.isci.2018.02.004_bib42) 2001; 276 Wang (10.1016/j.isci.2018.02.004_bib39) 2000; 275 Songyang (10.1016/j.isci.2018.02.004_bib35) 1995; 20 Bernardo (10.1016/j.isci.2018.02.004_bib4) 2003; 374 Caterina (10.1016/j.isci.2018.02.004_bib10) 2000; 275 Rapti (10.1016/j.isci.2018.02.004_bib29) 2006; 281 Sariahmetoglu (10.1016/j.isci.2018.02.004_bib32) 2007; 21 Sato (10.1016/j.isci.2018.02.004_bib33) 2009; 122 Batra (10.1016/j.isci.2018.02.004_bib1) 2013; 8 English (10.1016/j.isci.2018.02.004_bib15) 2006; 281 Egeblad (10.1016/j.isci.2018.02.004_bib14) 2002; 2 Nishi (10.1016/j.isci.2018.02.004_bib26) 2011; 19 DeRita (10.1016/j.isci.2018.02.004_bib11) 2016; 118 Tuuttila (10.1016/j.isci.2018.02.004_bib37) 1998; 284 Wingfield (10.1016/j.isci.2018.02.004_bib43) 1999; 274 Hornbeck (10.1016/j.isci.2018.02.004_bib16) 2015; 43 Dunn (10.1016/j.isci.2018.02.004_bib13) 2015; 12 Pinna (10.1016/j.isci.2018.02.004_bib28) 1996; 1314 Morrison (10.1016/j.isci.2018.02.004_bib24) 2001; 276 Kinoshita (10.1016/j.isci.2018.02.004_bib19) 1998; 273 Mollapour (10.1016/j.isci.2018.02.004_bib21) 2010; 37 Kessenbrock (10.1016/j.isci.2018.02.004_bib18) 2010; 141 Strongin (10.1016/j.isci.2018.02.004_bib36) 1995; 270 Betts (10.1016/j.isci.2018.02.004_bib5) 2003 Brown (10.1016/j.isci.2018.02.004_bib8) 1993; 43 Beebe (10.1016/j.isci.2018.02.004_bib2) 2013; 4 Brew (10.1016/j.isci.2018.02.004_bib7) 2010; 1803 Olson (10.1016/j.isci.2018.02.004_bib27) 1997; 272 Di Noto (10.1016/j.isci.2018.02.004_bib12) 2013; 8 Murphy (10.1016/j.isci.2018.02.004_bib25) 2011; 12 Visse (10.1016/j.isci.2018.02.004_bib38) 2003; 92 Morgunova (10.1016/j.isci.2018.02.004_bib22) 1999; 284 Zou (10.1016/j.isci.2018.02.004_bib44) 2016; 291 Bourboulia (10.1016/j.isci.2018.02.004_bib6) 2010; 20 Benham (10.1016/j.isci.2018.02.004_bib3) 2012; 4 Williams (10.1016/j.isci.2018.02.004_bib41) 2011; 286 Butler (10.1016/j.isci.2018.02.004_bib9) 1998; 273 Lafleur (10.1016/j.isci.2018.02.004_bib20) 2003; 553 Sharabi (10.1016/j.isci.2018.02.004_bib34) 2014; 9 Willenbrock (10.1016/j.isci.2018.02.004_bib40) 1993; 32 |
| References_xml | – start-page: 291 year: 2003 end-page: 316 ident: bib5 article-title: Amino acid properties and consequences of substitutions publication-title: Bioinformatics for Geneticists – volume: 2 start-page: 161 year: 2002 end-page: 174 ident: bib14 article-title: New functions for the matrix metalloproteinases in cancer progression publication-title: Nat. Rev. Cancer – volume: 286 start-page: 43405 year: 2011 end-page: 43416 ident: bib41 article-title: Phosphorylation of membrane type 1-matrix metalloproteinase (MT1-MMP) and its vesicle-associated membrane protein 7 (VAMP7)-dependent trafficking facilitate cell invasion and migration publication-title: J. Biol. Chem. – volume: 284 start-page: 1133 year: 1998 end-page: 1140 ident: bib37 article-title: Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 A resolution publication-title: J. Mol. Biol. – volume: 118 start-page: 66 year: 2016 end-page: 73 ident: bib11 article-title: c-Src, insulin-like growth factor I receptor, G-protein-coupled receptor kinases and focal adhesion kinase are enriched into prostate cancer cell exosomes publication-title: J. Cell Biochem. – volume: 553 start-page: 457 year: 2003 end-page: 463 ident: bib20 article-title: Selective involvement of TIMP-2 in the second activational cleavage of pro-MMP-2: refinement of the pro-MMP-2 activation mechanism publication-title: FEBS Lett. – volume: 276 start-page: 32966 year: 2001 end-page: 32970 ident: bib42 article-title: Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14 publication-title: J. Biol. Chem. – volume: 284 start-page: 1667 year: 1999 end-page: 1670 ident: bib22 article-title: Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed publication-title: Science – volume: 5 start-page: 143 year: 2014 end-page: 155 ident: bib30 article-title: Endocytosis and the Src family of non-receptor tyrosine kinases publication-title: Biomol. Concepts – volume: 12 start-page: 1006 year: 2015 end-page: 1018 ident: bib13 article-title: c-Abl mediated tyrosine phosphorylation of Aha1 activates its co-chaperone function in cancer cells publication-title: Cell Rep. – volume: 273 start-page: 16098 year: 1998 end-page: 16103 ident: bib19 article-title: TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads publication-title: J. Biol. Chem. – volume: 275 start-page: 26411 year: 2000 end-page: 26415 ident: bib39 article-title: TIMP-2 is required for efficient activation of proMMP-2 in vivo publication-title: J. Biol. Chem. – volume: 272 start-page: 29975 year: 1997 end-page: 29983 ident: bib27 article-title: Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2 publication-title: J. Biol. Chem. – volume: 69 start-page: 373 year: 2000 end-page: 398 ident: bib17 article-title: Protein tyrosine kinase structure and function publication-title: Annu. Rev. Biochem. – volume: 32 start-page: 4330 year: 1993 end-page: 4337 ident: bib40 article-title: The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A publication-title: Biochemistry – volume: 43 start-page: D512 year: 2015 end-page: D520 ident: bib16 article-title: PhosphoSitePlus, 2014: mutations, PTMs and recalibrations publication-title: Nucleic Acids Res. – volume: 141 start-page: 52 year: 2010 end-page: 67 ident: bib18 article-title: Matrix metalloproteinases: regulators of the tumor microenvironment publication-title: Cell – volume: 1803 start-page: 55 year: 2010 end-page: 71 ident: bib7 article-title: The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity publication-title: Biochim. Biophys. Acta – volume: 1314 start-page: 191 year: 1996 end-page: 225 ident: bib28 article-title: How do protein kinases recognize their substrates? publication-title: Biochim. Biophys. Acta – volume: 324 start-page: 1155 year: 2004 end-page: 1164 ident: bib31 article-title: Src protein-tyrosine kinase structure and regulation publication-title: Biochem. Biophys. Res. Commun. – volume: 270 start-page: 5331 year: 1995 end-page: 5338 ident: bib36 article-title: Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease publication-title: J. Biol. Chem. – volume: 281 start-page: 10337 year: 2006 end-page: 10346 ident: bib15 article-title: Individual Timp deficiencies differentially impact pro-MMP-2 activation publication-title: J. Biol. Chem. – volume: 99 start-page: 7414 year: 2002 end-page: 7419 ident: bib23 article-title: Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2 publication-title: Proc. Natl. Acad. Sci. USA – volume: 8 start-page: e70811 year: 2013 ident: bib12 article-title: C-src enriched serum microvesicles are generated in malignant plasma cell dyscrasia publication-title: PLoS One – volume: 20 start-page: 470 year: 1995 end-page: 475 ident: bib35 article-title: Recognition and specificity in protein tyrosine kinase-mediated signalling publication-title: Trends Biochem. Sci. – volume: 4 start-page: a012872 year: 2012 ident: bib3 article-title: Protein secretion and the endoplasmic reticulum publication-title: Cold Spring Harb. Perspect. Biol. – volume: 281 start-page: 23386 year: 2006 end-page: 23394 ident: bib29 article-title: Characterization of the AB loop region of TIMP-2. Involvement in pro-MMP-2 activation publication-title: J. Biol. Chem. – volume: 92 start-page: 827 year: 2003 end-page: 839 ident: bib38 article-title: Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry publication-title: Circ. Res. – volume: 274 start-page: 21362 year: 1999 end-page: 21368 ident: bib43 article-title: Biophysical and functional characterization of full-length, recombinant human tissue inhibitor of metalloproteinases-2 (TIMP-2) produced in publication-title: J. Biol. Chem. – volume: 20 start-page: 161 year: 2010 end-page: 168 ident: bib6 article-title: Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): positive and negative regulators in tumor cell adhesion publication-title: Semin. Cancer Biol. – volume: 273 start-page: 871 year: 1998 end-page: 880 ident: bib9 article-title: The TIMP2 membrane type 1 metalloproteinase “receptor” regulates the concentration and efficient activation of progelatinase A. A kinetic study publication-title: J. Biol. Chem. – volume: 4 start-page: 1065 year: 2013 end-page: 1074 ident: bib2 article-title: Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors publication-title: Oncotarget – volume: 8 start-page: e75836 year: 2013 ident: bib1 article-title: Matrix metalloproteinase-10/TIMP-2 structure and analyses define conserved core interactions and diverse exosite interactions in MMP/TIMP complexes publication-title: PLoS One – volume: 43 start-page: 163 year: 1993 end-page: 170 ident: bib8 article-title: Cellular activation of the 72 kDa type IV procollagenase/TIMP-2 complex publication-title: Kidney Int. – volume: 122 start-page: 965 year: 2009 end-page: 975 ident: bib33 article-title: Differential trafficking of Src, Lyn, Yes and Fyn is specified by the state of palmitoylation in the SH4 domain publication-title: J. Cell Sci. – volume: 9 start-page: e93712 year: 2014 ident: bib34 article-title: Affinity- and specificity-enhancing mutations are frequent in multispecific interactions between TIMP2 and MMPs publication-title: PLoS One – volume: 291 start-page: 11348 year: 2016 end-page: 11358 ident: bib44 article-title: Thermodynamic basis of selectivity in the interactions of tissue inhibitors of metalloproteinases N-domains with matrix Metalloproteinases-1, -3, and -14 publication-title: J. Biol. Chem. – volume: 275 start-page: 26416 year: 2000 end-page: 26422 ident: bib10 article-title: Inactivating mutation of the mouse tissue inhibitor of metalloproteinases-2(Timp-2) gene alters proMMP-2 activation publication-title: J. Biol. Chem. – volume: 21 start-page: 2486 year: 2007 end-page: 2495 ident: bib32 article-title: Regulation of matrix metalloproteinase-2 (MMP-2) activity by phosphorylation publication-title: FASEB J. – volume: 374 start-page: 739 year: 2003 end-page: 745 ident: bib4 article-title: TIMP-2 (tissue inhibitor of metalloproteinase-2) regulates MMP-2 (matrix metalloproteinase-2) activity in the extracellular environment after pro-MMP-2 activation by MT1 (membrane type 1)-MMP publication-title: Biochem. J. – volume: 37 start-page: 333 year: 2010 end-page: 343 ident: bib21 article-title: Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function publication-title: Mol. Cell – volume: 276 start-page: 47402 year: 2001 end-page: 47410 ident: bib24 article-title: Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway publication-title: J. Biol. Chem. – volume: 12 start-page: 233 year: 2011 ident: bib25 article-title: Tissue inhibitors of metalloproteinases publication-title: Genome Biol. – volume: 19 start-page: 1807 year: 2011 end-page: 1815 ident: bib26 article-title: Phosphorylation in protein-protein binding: effect on stability and function publication-title: Structure – volume: 2 start-page: 161 year: 2002 ident: 10.1016/j.isci.2018.02.004_bib14 article-title: New functions for the matrix metalloproteinases in cancer progression publication-title: Nat. Rev. Cancer doi: 10.1038/nrc745 – volume: 43 start-page: 163 year: 1993 ident: 10.1016/j.isci.2018.02.004_bib8 article-title: Cellular activation of the 72 kDa type IV procollagenase/TIMP-2 complex publication-title: Kidney Int. doi: 10.1038/ki.1993.27 – volume: 20 start-page: 161 year: 2010 ident: 10.1016/j.isci.2018.02.004_bib6 article-title: Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): positive and negative regulators in tumor cell adhesion publication-title: Semin. Cancer Biol. doi: 10.1016/j.semcancer.2010.05.002 – volume: 273 start-page: 871 year: 1998 ident: 10.1016/j.isci.2018.02.004_bib9 article-title: The TIMP2 membrane type 1 metalloproteinase “receptor” regulates the concentration and efficient activation of progelatinase A. A kinetic study publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.2.871 – volume: 284 start-page: 1133 year: 1998 ident: 10.1016/j.isci.2018.02.004_bib37 article-title: Three-dimensional structure of human tissue inhibitor of metalloproteinases-2 at 2.1 A resolution publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1998.2223 – volume: 374 start-page: 739 year: 2003 ident: 10.1016/j.isci.2018.02.004_bib4 article-title: TIMP-2 (tissue inhibitor of metalloproteinase-2) regulates MMP-2 (matrix metalloproteinase-2) activity in the extracellular environment after pro-MMP-2 activation by MT1 (membrane type 1)-MMP publication-title: Biochem. J. doi: 10.1042/bj20030557 – volume: 141 start-page: 52 year: 2010 ident: 10.1016/j.isci.2018.02.004_bib18 article-title: Matrix metalloproteinases: regulators of the tumor microenvironment publication-title: Cell doi: 10.1016/j.cell.2010.03.015 – volume: 37 start-page: 333 year: 2010 ident: 10.1016/j.isci.2018.02.004_bib21 article-title: Swe1Wee1-dependent tyrosine phosphorylation of Hsp90 regulates distinct facets of chaperone function publication-title: Mol. Cell doi: 10.1016/j.molcel.2010.01.005 – volume: 553 start-page: 457 year: 2003 ident: 10.1016/j.isci.2018.02.004_bib20 article-title: Selective involvement of TIMP-2 in the second activational cleavage of pro-MMP-2: refinement of the pro-MMP-2 activation mechanism publication-title: FEBS Lett. doi: 10.1016/S0014-5793(03)01094-9 – volume: 118 start-page: 66 year: 2016 ident: 10.1016/j.isci.2018.02.004_bib11 article-title: c-Src, insulin-like growth factor I receptor, G-protein-coupled receptor kinases and focal adhesion kinase are enriched into prostate cancer cell exosomes publication-title: J. Cell Biochem. doi: 10.1002/jcb.25611 – volume: 4 start-page: 1065 year: 2013 ident: 10.1016/j.isci.2018.02.004_bib2 article-title: Posttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitors publication-title: Oncotarget doi: 10.18632/oncotarget.1099 – volume: 291 start-page: 11348 year: 2016 ident: 10.1016/j.isci.2018.02.004_bib44 article-title: Thermodynamic basis of selectivity in the interactions of tissue inhibitors of metalloproteinases N-domains with matrix Metalloproteinases-1, -3, and -14 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M116.720250 – volume: 69 start-page: 373 year: 2000 ident: 10.1016/j.isci.2018.02.004_bib17 article-title: Protein tyrosine kinase structure and function publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.69.1.373 – volume: 20 start-page: 470 year: 1995 ident: 10.1016/j.isci.2018.02.004_bib35 article-title: Recognition and specificity in protein tyrosine kinase-mediated signalling publication-title: Trends Biochem. Sci. doi: 10.1016/S0968-0004(00)89103-3 – volume: 21 start-page: 2486 year: 2007 ident: 10.1016/j.isci.2018.02.004_bib32 article-title: Regulation of matrix metalloproteinase-2 (MMP-2) activity by phosphorylation publication-title: FASEB J. doi: 10.1096/fj.06-7938com – volume: 276 start-page: 32966 year: 2001 ident: 10.1016/j.isci.2018.02.004_bib42 article-title: Tyrosine 36 plays a critical role in the interaction of the AB loop of tissue inhibitor of metalloproteinases-2 with matrix metalloproteinase-14 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M101843200 – start-page: 291 year: 2003 ident: 10.1016/j.isci.2018.02.004_bib5 article-title: Amino acid properties and consequences of substitutions – volume: 284 start-page: 1667 year: 1999 ident: 10.1016/j.isci.2018.02.004_bib22 article-title: Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed publication-title: Science doi: 10.1126/science.284.5420.1667 – volume: 12 start-page: 233 year: 2011 ident: 10.1016/j.isci.2018.02.004_bib25 article-title: Tissue inhibitors of metalloproteinases publication-title: Genome Biol. doi: 10.1186/gb-2011-12-11-233 – volume: 43 start-page: D512 year: 2015 ident: 10.1016/j.isci.2018.02.004_bib16 article-title: PhosphoSitePlus, 2014: mutations, PTMs and recalibrations publication-title: Nucleic Acids Res. doi: 10.1093/nar/gku1267 – volume: 4 start-page: a012872 year: 2012 ident: 10.1016/j.isci.2018.02.004_bib3 article-title: Protein secretion and the endoplasmic reticulum publication-title: Cold Spring Harb. Perspect. Biol. doi: 10.1101/cshperspect.a012872 – volume: 9 start-page: e93712 year: 2014 ident: 10.1016/j.isci.2018.02.004_bib34 article-title: Affinity- and specificity-enhancing mutations are frequent in multispecific interactions between TIMP2 and MMPs publication-title: PLoS One doi: 10.1371/journal.pone.0093712 – volume: 275 start-page: 26411 year: 2000 ident: 10.1016/j.isci.2018.02.004_bib39 article-title: TIMP-2 is required for efficient activation of proMMP-2 in vivo publication-title: J. Biol. Chem. doi: 10.1074/jbc.M001270200 – volume: 8 start-page: e75836 year: 2013 ident: 10.1016/j.isci.2018.02.004_bib1 article-title: Matrix metalloproteinase-10/TIMP-2 structure and analyses define conserved core interactions and diverse exosite interactions in MMP/TIMP complexes publication-title: PLoS One doi: 10.1371/journal.pone.0075836 – volume: 276 start-page: 47402 year: 2001 ident: 10.1016/j.isci.2018.02.004_bib24 article-title: Cellular activation of MMP-2 (gelatinase A) by MT2-MMP occurs via a TIMP-2-independent pathway publication-title: J. Biol. Chem. doi: 10.1074/jbc.M108643200 – volume: 99 start-page: 7414 year: 2002 ident: 10.1016/j.isci.2018.02.004_bib23 article-title: Structural insight into the complex formation of latent matrix metalloproteinase 2 with tissue inhibitor of metalloproteinase 2 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.102185399 – volume: 281 start-page: 23386 year: 2006 ident: 10.1016/j.isci.2018.02.004_bib29 article-title: Characterization of the AB loop region of TIMP-2. Involvement in pro-MMP-2 activation publication-title: J. Biol. Chem. doi: 10.1074/jbc.M604423200 – volume: 270 start-page: 5331 year: 1995 ident: 10.1016/j.isci.2018.02.004_bib36 article-title: Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease publication-title: J. Biol. Chem. doi: 10.1074/jbc.270.10.5331 – volume: 281 start-page: 10337 year: 2006 ident: 10.1016/j.isci.2018.02.004_bib15 article-title: Individual Timp deficiencies differentially impact pro-MMP-2 activation publication-title: J. Biol. Chem. doi: 10.1074/jbc.M512009200 – volume: 286 start-page: 43405 year: 2011 ident: 10.1016/j.isci.2018.02.004_bib41 article-title: Phosphorylation of membrane type 1-matrix metalloproteinase (MT1-MMP) and its vesicle-associated membrane protein 7 (VAMP7)-dependent trafficking facilitate cell invasion and migration publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111.297069 – volume: 12 start-page: 1006 year: 2015 ident: 10.1016/j.isci.2018.02.004_bib13 article-title: c-Abl mediated tyrosine phosphorylation of Aha1 activates its co-chaperone function in cancer cells publication-title: Cell Rep. doi: 10.1016/j.celrep.2015.07.004 – volume: 19 start-page: 1807 year: 2011 ident: 10.1016/j.isci.2018.02.004_bib26 article-title: Phosphorylation in protein-protein binding: effect on stability and function publication-title: Structure doi: 10.1016/j.str.2011.09.021 – volume: 1803 start-page: 55 year: 2010 ident: 10.1016/j.isci.2018.02.004_bib7 article-title: The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity publication-title: Biochim. Biophys. Acta doi: 10.1016/j.bbamcr.2010.01.003 – volume: 122 start-page: 965 year: 2009 ident: 10.1016/j.isci.2018.02.004_bib33 article-title: Differential trafficking of Src, Lyn, Yes and Fyn is specified by the state of palmitoylation in the SH4 domain publication-title: J. Cell Sci. doi: 10.1242/jcs.034843 – volume: 92 start-page: 827 year: 2003 ident: 10.1016/j.isci.2018.02.004_bib38 article-title: Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry publication-title: Circ. Res. doi: 10.1161/01.RES.0000070112.80711.3D – volume: 5 start-page: 143 year: 2014 ident: 10.1016/j.isci.2018.02.004_bib30 article-title: Endocytosis and the Src family of non-receptor tyrosine kinases publication-title: Biomol. Concepts doi: 10.1515/bmc-2014-0003 – volume: 324 start-page: 1155 year: 2004 ident: 10.1016/j.isci.2018.02.004_bib31 article-title: Src protein-tyrosine kinase structure and regulation publication-title: Biochem. Biophys. Res. Commun. doi: 10.1016/j.bbrc.2004.09.171 – volume: 274 start-page: 21362 year: 1999 ident: 10.1016/j.isci.2018.02.004_bib43 publication-title: J. Biol. Chem. doi: 10.1074/jbc.274.30.21362 – volume: 8 start-page: e70811 year: 2013 ident: 10.1016/j.isci.2018.02.004_bib12 article-title: C-src enriched serum microvesicles are generated in malignant plasma cell dyscrasia publication-title: PLoS One doi: 10.1371/journal.pone.0070811 – volume: 273 start-page: 16098 year: 1998 ident: 10.1016/j.isci.2018.02.004_bib19 article-title: TIMP-2 promotes activation of progelatinase A by membrane-type 1 matrix metalloproteinase immobilized on agarose beads publication-title: J. Biol. Chem. doi: 10.1074/jbc.273.26.16098 – volume: 1314 start-page: 191 year: 1996 ident: 10.1016/j.isci.2018.02.004_bib28 article-title: How do protein kinases recognize their substrates? publication-title: Biochim. Biophys. Acta doi: 10.1016/S0167-4889(96)00083-3 – volume: 275 start-page: 26416 year: 2000 ident: 10.1016/j.isci.2018.02.004_bib10 article-title: Inactivating mutation of the mouse tissue inhibitor of metalloproteinases-2(Timp-2) gene alters proMMP-2 activation publication-title: J. Biol. Chem. doi: 10.1074/jbc.M001271200 – volume: 272 start-page: 29975 year: 1997 ident: 10.1016/j.isci.2018.02.004_bib27 article-title: Kinetic analysis of the binding of human matrix metalloproteinase-2 and -9 to tissue inhibitor of metalloproteinase (TIMP)-1 and TIMP-2 publication-title: J. Biol. Chem. doi: 10.1074/jbc.272.47.29975 – volume: 32 start-page: 4330 year: 1993 ident: 10.1016/j.isci.2018.02.004_bib40 article-title: The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A publication-title: Biochemistry doi: 10.1021/bi00067a023 |
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| Title | Extracellular Phosphorylation of TIMP-2 by Secreted c-Src Tyrosine Kinase Controls MMP-2 Activity |
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