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Volumn 127, Issue 9, 2014, Pages 1875-1886

The role of the interaction of the vinculin proline-rich linker region with vinexin α in sensing the stiffness of the extracellular matrix

Author keywords

Extracellular matrix; Mechanotransduction; Stiffness; Vinculin

Indexed keywords

BINDING PROTEIN; F ACTIN; PAXILLIN; PROLINE RICH PROTEIN; UNCLASSIFIED DRUG; VINCULIN; VINEXIN ALPHA; MUSCLE PROTEIN; SH3D4 PROTEIN, MOUSE;

EID: 84899715850     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.133645     Document Type: Article
Times cited : (48)

References (57)
  • 5
    • 79151482119 scopus 로고    scopus 로고
    • Vinculin, an adapter protein in control of cell adhesion signalling
    • Carisey, A. and Ballestrem, C. (2011). Vinculin, an adapter protein in control of cell adhesion signalling. Eur. J. Cell Biol. 90, 157-163.
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 157-163
    • Carisey, A.1    Ballestrem, C.2
  • 7
    • 33846030511 scopus 로고    scopus 로고
    • Coincidence of actin filaments and talin is required to activate vinculin
    • Chen, H., Choudhury, D. M. and Craig, S. W. (2006). Coincidence of actin filaments and talin is required to activate vinculin. J. Biol. Chem. 281, 40389-40398.
    • (2006) J. Biol. Chem. , vol.281 , pp. 40389-40398
    • Chen, H.1    Choudhury, D.M.2    Craig, S.W.3
  • 8
    • 18844369343 scopus 로고    scopus 로고
    • Spatial distribution and functional significance of activated vinculin in living cells
    • Chen, H., Cohen, D. M., Choudhury, D. M., Kioka, N. and Craig, S. W. (2005). Spatial distribution and functional significance of activated vinculin in living cells. J. Cell Biol. 169, 459-470.
    • (2005) J. Cell Biol. , vol.169 , pp. 459-470
    • Chen, H.1    Cohen, D.M.2    Choudhury, D.M.3    Kioka, N.4    Craig, S.W.5
  • 9
    • 20444492339 scopus 로고    scopus 로고
    • Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin
    • Cohen, D. M., Chen, H., Johnson, R. P., Choudhury, B. and Craig, S. W. (2005). Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin. J. Biol. Chem. 280, 17109-17117.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17109-17117
    • Cohen, D.M.1    Chen, H.2    Johnson, R.P.3    Choudhury, B.4    Craig, S.W.5
  • 10
    • 33744929406 scopus 로고    scopus 로고
    • A conformational switch in vinculin drives formation and dynamics of a talinvinculin complex at focal adhesions
    • Cohen, D. M., Kutscher, B., Chen, H., Murphy, D. B. and Craig, S. W. (2006). A conformational switch in vinculin drives formation and dynamics of a talinvinculin complex at focal adhesions. J. Biol. Chem. 281, 16006-16015.
    • (2006) J. Biol. Chem. , vol.281 , pp. 16006-16015
    • Cohen, D.M.1    Kutscher, B.2    Chen, H.3    Murphy, D.B.4    Craig, S.W.5
  • 11
    • 33644792639 scopus 로고    scopus 로고
    • Bulk and micropatterned conjugation of extracellular matrix proteins to characterized polyacrylamide substrates for cell mechanotransduction assays
    • Damljanović, V., Lagerholm, B. C. and Jacobson, K. (2005). Bulk and micropatterned conjugation of extracellular matrix proteins to characterized polyacrylamide substrates for cell mechanotransduction assays. Biotechniques 39, 847-851.
    • (2005) Biotechniques , vol.39 , pp. 847-851
    • Damljanović, V.1    Lagerholm, B.C.2    Jacobson, K.3
  • 13
    • 0037049555 scopus 로고    scopus 로고
    • Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion
    • DeMali, K. A., Barlow, C. A. and Burridge, K. (2002). Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159, 881-891.
    • (2002) J. Cell Biol. , vol.159 , pp. 881-891
    • DeMali, K.A.1    Barlow, C.A.2    Burridge, K.3
  • 14
    • 67649920749 scopus 로고    scopus 로고
    • Growth factors, matrices, and forces combine and control stem cells
    • Discher, D. E., Mooney, D. J. and Zandstra, P. W. (2009). Growth factors, matrices, and forces combine and control stem cells. Science 324, 1673-1677.
    • (2009) Science , vol.324 , pp. 1673-1677
    • Discher, D.E.1    Mooney, D.J.2    Zandstra, P.W.3
  • 15
    • 0032499609 scopus 로고    scopus 로고
    • Measuring the elastic properties of thin polymer films with the atomic force microscope
    • Domke, J. and Radmacher, M. (1998). Measuring the elastic properties of thin polymer films with the atomic force microscope. Langmuir 14, 3320-3325.
    • (1998) Langmuir , vol.14 , pp. 3320-3325
    • Domke, J.1    Radmacher, M.2
  • 16
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • Engler, A. J., Sen, S., Sweeney, H. L. and Discher, D. E. (2006). Matrix elasticity directs stem cell lineage specification. Cell 126, 677-689.
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 17
    • 0021244964 scopus 로고
    • Epithelial cytoskeletal frameworkand nuclear matrix-intermediate filament scaffold: three-dimensional organization and protein composition
    • Fey, E. G., Wan, K. M. and Penman, S. (1984). Epithelial cytoskeletal frameworkand nuclear matrix-intermediate filament scaffold: three-dimensional organization and protein composition. J. Cell Biol. 98, 1973-1984.
    • (1984) J. Cell Biol. , vol.98 , pp. 1973-1984
    • Fey, E.G.1    Wan, K.M.2    Penman, S.3
  • 18
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls alpha5beta1 function
    • Friedland, J. C., Lee, M. H. and Boettiger, D. (2009). Mechanically activated integrin switch controls alpha5beta1 function. Science 323, 642-644.
    • (2009) Science , vol.323 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 20
    • 0031817205 scopus 로고    scopus 로고
    • Differences in elasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy
    • Goldmann, W. H., Galneder, R., Ludwig, M., Xu, W., Adamson, E. D., Wang, N. and Ezzell, R. M. (1998). Differences in elasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy. Exp. Cell Res. 239, 235-242.
    • (1998) Exp. Cell Res. , vol.239 , pp. 235-242
    • Goldmann, W.H.1    Galneder, R.2    Ludwig, M.3    Xu, W.4    Adamson, E.D.5    Wang, N.6    Ezzell, R.M.7
  • 21
    • 77958171400 scopus 로고    scopus 로고
    • A molecular dynamics investigation of vinculin activation
    • Golji, J. and Mofrad, M. R. (2010). A molecular dynamics investigation of vinculin activation. Biophys. J. 99, 1073-1081.
    • (2010) Biophys. J. , vol.99 , pp. 1073-1081
    • Golji, J.1    Mofrad, M.R.2
  • 23
    • 52949123215 scopus 로고    scopus 로고
    • pCold-GST vector: a novel cold-shock vector containing GST tag for soluble protein production
    • Hayashi, K. and Kojima, C. (2008). pCold-GST vector: a novel cold-shock vector containing GST tag for soluble protein production. Protein Expr. Purif. 62, 120-127.
    • (2008) Protein Expr. Purif. , vol.62 , pp. 120-127
    • Hayashi, K.1    Kojima, C.2
  • 24
    • 36849069902 scopus 로고    scopus 로고
    • Vinculin controls focal adhesion formation by direct interactions with talin and actin
    • Humphries, J. D., Wang, P., Streuli, C., Geiger, B., Humphries, M. J. and Ballestrem, C. (2007). Vinculin controls focal adhesion formation by direct interactions with talin and actin. J. Cell Biol. 179, 1043-1057.
    • (2007) J. Cell Biol. , vol.179 , pp. 1043-1057
    • Humphries, J.D.1    Wang, P.2    Streuli, C.3    Geiger, B.4    Humphries, M.J.5    Ballestrem, C.6
  • 25
    • 0347717894 scopus 로고    scopus 로고
    • Vinculin activation by talin through helical bundle conversion
    • Izard, T., Evans, G., Borgon, R. A., Rush, C. L., Bricogne, G. and Bois, P. R. (2004). Vinculin activation by talin through helical bundle conversion. Nature 427, 171-175.
    • (2004) Nature , vol.427 , pp. 171-175
    • Izard, T.1    Evans, G.2    Borgon, R.A.3    Rush, C.L.4    Bricogne, G.5    Bois, P.R.6
  • 27
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • Johnson, R. P. and Craig, S. W. (1995). F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature 373, 261-264.
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 28
    • 0035979221 scopus 로고    scopus 로고
    • The sorbin homology domain: a motif for the targeting of proteins to lipid rafts
    • Kimura, A., Baumann, C. A., Chiang, S. H. and Saltiel, A. R. (2001). The sorbin homology domain: a motif for the targeting of proteins to lipid rafts. Proc. Natl. Acad. Sci. USA 98, 9098-9103.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9098-9103
    • Kimura, A.1    Baumann, C.A.2    Chiang, S.H.3    Saltiel, A.R.4
  • 31
    • 0036257343 scopus 로고    scopus 로고
    • Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction.
    • Kioka, N., Ueda, K. and Amachi, T. (2002). Vinexin, CAP/ponsin, ArgBP2: a novel adaptor protein family regulating cytoskeletal organization and signal transduction. Cell Struct. Funct. 27, 1-7.
    • (2002) Cell Struct. Funct. , vol.27 , pp. 1-7
    • Kioka, N.1    Ueda, K.2    Amachi, T.3
  • 32
    • 78649809572 scopus 로고    scopus 로고
    • Vinexinb, an atypical "sensor"of retinoic acid receptor gamma signaling: union and sequestration, separation, and phosphorylation
    • Lalevee, S., Bour, G., Quinternet, M., Samarut, E., Kessler, P., Vitorino, M., Bruck, N., Delsuc, M. A., Vonesch, J. L., Kieffer, B. et al. (2010). Vinexinb, an atypical "sensor"of retinoic acid receptor gamma signaling: union and sequestration, separation, and phosphorylation. FASEB J. 24, 4523-4534.
    • (2010) FASEB J , vol.24 , pp. 4523-4534
    • Lalevee, S.1    Bour, G.2    Quinternet, M.3    Samarut, E.4    Kessler, P.5    Vitorino, M.6    Bruck, N.7    Delsuc, M.A.8    Vonesch, J.L.9    Kieffer, B.10
  • 33
    • 0031054498 scopus 로고    scopus 로고
    • Vinculin and talin: kinetics of entry and exit from the cytoskeletal pool
    • Lee, S. and Otto, J. J. (1997). Vinculin and talin: kinetics of entry and exit from the cytoskeletal pool. Cell Motil. Cytoskeleton 36, 101-111.
    • (1997) Cell Motil. Cytoskeleton , vol.36 , pp. 101-111
    • Lee, S.1    Otto, J.J.2
  • 34
    • 0033917881 scopus 로고    scopus 로고
    • Cell movement is guided by the rigidity of the substrate
    • Lo, C. M., Wang, H. B., Dembo, M. and Wang, Y. L. (2000). Cell movement is guided by the rigidity of the substrate. Biophys. J. 79, 144-152.
    • (2000) Biophys. J. , vol.79 , pp. 144-152
    • Lo, C.M.1    Wang, H.B.2    Dembo, M.3    Wang, Y.L.4
  • 35
    • 84855975404 scopus 로고    scopus 로고
    • Abl-1-bridged tyrosine phosphorylation of VASP by Abelson kinase impairs association of VASP to focal adhesions and regulates leukaemic cell adhesion
    • Maruoka, M., Sato, M., Yuan, Y., Ichiba, M., Fujii, R., Ogawa, T., Ishida-Kitagawa, N., Takeya, T. and Watanabe, N. (2012). Abl-1-bridged tyrosine phosphorylation of VASP by Abelson kinase impairs association of VASP to focal adhesions and regulates leukaemic cell adhesion. Biochem. J. 441, 889-899.
    • (2012) Biochem. J. , vol.441 , pp. 889-899
    • Maruoka, M.1    Sato, M.2    Yuan, Y.3    Ichiba, M.4    Fujii, R.5    Ogawa, T.6    Ishida-Kitagawa, N.7    Takeya, T.8    Watanabe, N.9
  • 37
    • 33645771745 scopus 로고    scopus 로고
    • Protein kinase A-dependent increase in WAVE2 expression induced by the focal adhesion protein vinexin
    • Mitsushima, M., Sezaki, T., Akahane, R., Ueda, K., Suetsugu, S., Takenawa, T. and Kioka, N. (2006a). Protein kinase A-dependent increase in WAVE2 expression induced by the focal adhesion protein vinexin. Genes Cells 11, 281-292.
    • (2006) Genes Cells , vol.11 , pp. 281-292
    • Mitsushima, M.1    Sezaki, T.2    Akahane, R.3    Ueda, K.4    Suetsugu, S.5    Takenawa, T.6    Kioka, N.7
  • 38
    • 4544227784 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin
    • Mitsushima, M., Suwa, A., Amachi, T., Ueda, K. and Kioka, N. (2004). Extracellular signal-regulated kinase activated by epidermal growth factor and cell adhesion interacts with and phosphorylates vinexin. J. Biol. Chem. 279, 34570-34577.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34570-34577
    • Mitsushima, M.1    Suwa, A.2    Amachi, T.3    Ueda, K.4    Kioka, N.5
  • 39
  • 41
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: integrating cytoskeletal dynamics and cellular tension
    • Parsons, J. T., Horwitz, A. R. and Schwartz, M. A. (2010). Cell adhesion: integrating cytoskeletal dynamics and cellular tension. Nat. Rev. Mol. Cell Biol. 11, 633-643.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schwartz, M.A.3
  • 42
    • 77949754056 scopus 로고    scopus 로고
    • Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation
    • Pasapera, A. M., Schneider, I. C., Rericha, E., Schlaepfer, D. D. and Waterman, C. M. (2010). Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation. J. Cell Biol. 188, 877-890.
    • (2010) J. Cell Biol. , vol.188 , pp. 877-890
    • Pasapera, A.M.1    Schneider, I.C.2    Rericha, E.3    Schlaepfer, D.D.4    Waterman, C.M.5
  • 44
    • 0031417774 scopus 로고    scopus 로고
    • Periplakin, a novel component of cornified envelopes and desmosomes that belongs to the plakin family and forms complexes with envoplakin
    • Ruhrberg, C., Hajibagheri, M. A., Parry, D. A. and Watt, F. M. (1997). Periplakin, a novel component of cornified envelopes and desmosomes that belongs to the plakin family and forms complexes with envoplakin. J. Cell Biol. 139, 1835-1849.
    • (1997) J. Cell Biol. , vol.139 , pp. 1835-1849
    • Ruhrberg, C.1    Hajibagheri, M.A.2    Parry, D.A.3    Watt, F.M.4
  • 46
    • 84881396465 scopus 로고    scopus 로고
    • Site-specific inhibitory mechanism for amyloid b42 aggregation by catechol-type flavonoids targeting the Lys residues
    • Sato, M., Murakami, K., Uno, M., Nakagawa, Y., Katayama, S., Akagi, K., Masuda, Y., Takegoshi, K. and Irie, K. (2013). Site-specific inhibitory mechanism for amyloid b42 aggregation by catechol-type flavonoids targeting the Lys residues. J. Biol. Chem. 288, 23212-23224.
    • (2013) J. Biol. Chem. , vol.288 , pp. 23212-23224
    • Sato, M.1    Murakami, K.2    Uno, M.3    Nakagawa, Y.4    Katayama, S.5    Akagi, K.6    Masuda, Y.7    Takegoshi, K.8    Irie, K.9
  • 47
    • 0037128202 scopus 로고    scopus 로고
    • Force transduction by Triton cytoskeletons
    • Sawada, Y. and Sheetz, M. P. (2002). Force transduction by Triton cytoskeletons. J. Cell Biol. 156, 609-615.
    • (2002) J. Cell Biol. , vol.156 , pp. 609-615
    • Sawada, Y.1    Sheetz, M.P.2
  • 49
    • 84863862833 scopus 로고    scopus 로고
    • Mammary gland ECM remodeling, stiffness, and mechanosignaling in normal development and tumor progression
    • Schedin, P. and Keely, P. J. (2011). Mammary gland ECM remodeling, stiffness, and mechanosignaling in normal development and tumor progression. Cold Spring Harb. Perspect. Biol. 3, a003228.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Schedin, P.1    Keely, P.J.2
  • 50
    • 0037066734 scopus 로고    scopus 로고
    • Vinexin beta regulates the anchorage dependence of ERK2 activation stimulated by epidermal growth factor
    • Suwa, A., Mitsushima, M., Ito, T., Akamatsu, M., Ueda, K., Amachi, T. and Kioka, N. (2002). Vinexin beta regulates the anchorage dependence of ERK2 activation stimulated by epidermal growth factor. J. Biol. Chem. 277, 13053-13058.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13053-13058
    • Suwa, A.1    Mitsushima, M.2    Ito, T.3    Akamatsu, M.4    Ueda, K.5    Amachi, T.6    Kioka, N.7
  • 52
    • 84883840386 scopus 로고
    • Quantitative studies of the growth of mouse embryo cells in culture and their development into established lines
    • Todaro, G. J. and Green, H. (1963). Quantitative studies of the growth of mouse embryo cells in culture and their development into established lines. J. Cell Biol. 17, 299-313.
    • (1963) J. Cell Biol. , vol.17 , pp. 299-313
    • Todaro, G.J.1    Green, H.2
  • 53
    • 77953816876 scopus 로고    scopus 로고
    • Preparation of hydrogel substrates with tunable mechanical properties
    • Unit 10.16.1-10.16.16.
    • Tse, J. R. and Engler, A. J. (2010). Preparation of hydrogel substrates with tunable mechanical properties. Current Protocols in Cell Biology 10, Unit 10.16.1-10.16.16.
    • (2010) Current Protocols in Cell Biology 10
    • Tse, J.R.1    Engler, A.J.2
  • 54
    • 67651017495 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of vinexin in v-Src-transformed cells attenuates the affinity for vinculin
    • Umemoto, T., Tanaka, K., Ueda, K. and Kioka, N. (2009). Tyrosine phosphorylation of vinexin in v-Src-transformed cells attenuates the affinity for vinculin. Biochem. Biophys. Res. Commun. 387, 191-195.
    • (2009) Biochem. Biophys. Res. Commun. , vol.387 , pp. 191-195
    • Umemoto, T.1    Tanaka, K.2    Ueda, K.3    Kioka, N.4
  • 55
    • 0037821783 scopus 로고    scopus 로고
    • Interaction of lp-dlg/KIAA0583, a membrane-associated guanylate kinase family protein, with vinexin and beta-catenin at sites of cell-cell contact
    • Wakabayashi, M., Ito, T., Mitsushima, M., Aizawa, S., Ueda, K., Amachi, T. and Kioka, N. (2003). Interaction of lp-dlg/KIAA0583, a membrane-associated guanylate kinase family protein, with vinexin and beta-catenin at sites of cell-cell contact. J. Biol. Chem. 278, 21709-21714.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21709-21714
    • Wakabayashi, M.1    Ito, T.2    Mitsushima, M.3    Aizawa, S.4    Ueda, K.5    Amachi, T.6    Kioka, N.7
  • 56
    • 79955538660 scopus 로고    scopus 로고
    • Actomyosingenerated tension controls the molecular kinetics of focal adhesions
    • Wolfenson, H., Bershadsky, A., Henis, Y. I. and Geiger, B. (2011). Actomyosingenerated tension controls the molecular kinetics of focal adhesions. J. Cell Sci. 124, 1425-1432.
    • (2011) J. Cell Sci. , vol.124 , pp. 1425-1432
    • Wolfenson, H.1    Bershadsky, A.2    Henis, Y.I.3    Geiger, B.4


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