메뉴 건너뛰기




Volumn 102, Issue 9, 2012, Pages 2022-2030

Phosphorylation primes vinculin for activation

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN KINASE; VINCULIN;

EID: 84860475799     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.01.062     Document Type: Article
Times cited : (38)

References (48)
  • 2
    • 66849101632 scopus 로고    scopus 로고
    • Adhesion signaling - Crosstalk between integrins, Src and Rho
    • S. Huveneers, and E.H. Danen Adhesion signaling - crosstalk between integrins, Src and Rho J. Cell Sci. 122 2009 1059 1069
    • (2009) J. Cell Sci. , vol.122 , pp. 1059-1069
    • Huveneers, S.1    Danen, E.H.2
  • 3
    • 77955580383 scopus 로고    scopus 로고
    • Stretchy proteins on stretchy substrates: The important elements of integrin-mediated rigidity sensing
    • S.W. Moore, P. Roca-Cusachs, and M.P. Sheetz Stretchy proteins on stretchy substrates: the important elements of integrin-mediated rigidity sensing Dev. Cell 19 2010 194 206
    • (2010) Dev. Cell , vol.19 , pp. 194-206
    • Moore, S.W.1    Roca-Cusachs, P.2    Sheetz, M.P.3
  • 4
    • 68549112897 scopus 로고    scopus 로고
    • Mechanics, malignancy, and metastasis: The force journey of a tumor cell
    • S. Kumar, and V.M. Weaver Mechanics, malignancy, and metastasis: the force journey of a tumor cell Cancer Metastasis Rev. 28 2009 113 127
    • (2009) Cancer Metastasis Rev. , vol.28 , pp. 113-127
    • Kumar, S.1    Weaver, V.M.2
  • 5
    • 67651085772 scopus 로고    scopus 로고
    • Signal transduction by focal adhesion kinase in cancer
    • J. Zhao, and J.L. Guan Signal transduction by focal adhesion kinase in cancer Cancer Metastasis Rev. 28 2009 35 49
    • (2009) Cancer Metastasis Rev. , vol.28 , pp. 35-49
    • Zhao, J.1    Guan, J.L.2
  • 6
    • 78049361778 scopus 로고    scopus 로고
    • Mechanical integration of actin and adhesion dynamics in cell migration
    • M.L. Gardel, and I.C. Schneider C.M. Waterman Mechanical integration of actin and adhesion dynamics in cell migration Annu. Rev. Cell Dev. Biol. 26 2010 315 333
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 315-333
    • Gardel, M.L.1    Schneider, I.C.2    Waterman, C.M.3
  • 8
    • 33645780908 scopus 로고    scopus 로고
    • Mechanotransduction involving multimodular proteins: Converting force into biochemical signals
    • V. Vogel Mechanotransduction involving multimodular proteins: converting force into biochemical signals Annu. Rev. Biophys. Biomol. Struct. 35 2006 459 488
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 459-488
    • Vogel, V.1
  • 9
    • 0023710857 scopus 로고
    • A precursor of the focal contact in cultured fibroblasts
    • C.S. Izzard A precursor of the focal contact in cultured fibroblasts Cell Motil. Cytoskeleton 10 1988 137 142
    • (1988) Cell Motil. Cytoskeleton , vol.10 , pp. 137-142
    • Izzard, C.S.1
  • 10
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • C.G. Galbraith, K.M. Yamada, and M.P. Sheetz The relationship between force and focal complex development J. Cell Biol. 159 2002 695 705
    • (2002) J. Cell Biol. , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 12
    • 78751692682 scopus 로고    scopus 로고
    • Vinculin activation is necessary for complete talin binding
    • J. Golji, J. Lam, and M.R. Mofrad Vinculin activation is necessary for complete talin binding Biophys. J. 100 2011 332 340
    • (2011) Biophys. J. , vol.100 , pp. 332-340
    • Golji, J.1    Lam, J.2    Mofrad, M.R.3
  • 13
    • 36849069902 scopus 로고    scopus 로고
    • Vinculin controls focal adhesion formation by direct interactions with talin and actin
    • J.D. Humphries, and P. Wang C. Ballestrem Vinculin controls focal adhesion formation by direct interactions with talin and actin J. Cell Biol. 179 2007 1043 1057
    • (2007) J. Cell Biol. , vol.179 , pp. 1043-1057
    • Humphries, J.D.1    Wang, P.2    Ballestrem, C.3
  • 14
    • 30744465307 scopus 로고    scopus 로고
    • Three-dimensional structure of vinculin bound to actin filaments
    • M.E. Janssen, and E. Kim D. Hanein Three-dimensional structure of vinculin bound to actin filaments Mol. Cell 21 2006 271 281
    • (2006) Mol. Cell , vol.21 , pp. 271-281
    • Janssen, M.E.1    Kim, E.2    Hanein, D.3
  • 15
    • 0347717894 scopus 로고    scopus 로고
    • Vinculin activation by talin through helical bundle conversion
    • T. Izard, and G. Evans P.R. Bois Vinculin activation by talin through helical bundle conversion Nature 427 2004 171 175
    • (2004) Nature , vol.427 , pp. 171-175
    • Izard, T.1    Evans, G.2    Bois, P.R.3
  • 16
    • 20444492339 scopus 로고    scopus 로고
    • Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin
    • D.M. Cohen, and H. Chen S.W. Craig Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin J. Biol. Chem. 280 2005 17109 17117
    • (2005) J. Biol. Chem. , vol.280 , pp. 17109-17117
    • Cohen, D.M.1    Chen, H.2    Craig, S.W.3
  • 17
    • 77958171400 scopus 로고    scopus 로고
    • A molecular dynamics investigation of vinculin activation
    • J. Golji, and M.R. Mofrad A molecular dynamics investigation of vinculin activation Biophys. J. 99 2010 1073 1081
    • (2010) Biophys. J. , vol.99 , pp. 1073-1081
    • Golji, J.1    Mofrad, M.R.2
  • 18
    • 33846030511 scopus 로고    scopus 로고
    • Coincidence of actin filaments and talin is required to activate vinculin
    • H. Chen, D.M. Choudhury, and S.W. Craig Coincidence of actin filaments and talin is required to activate vinculin J. Biol. Chem. 281 2006 40389 40398
    • (2006) J. Biol. Chem. , vol.281 , pp. 40389-40398
    • Chen, H.1    Choudhury, D.M.2    Craig, S.W.3
  • 19
    • 34047245107 scopus 로고    scopus 로고
    • The Helicobacter pylori CagA protein disrupts matrix adhesion of gastric epithelial cells by dephosphorylation of vinculin
    • S. Moese, and M. Selbach T.F. Meyer The Helicobacter pylori CagA protein disrupts matrix adhesion of gastric epithelial cells by dephosphorylation of vinculin Cell. Microbiol. 9 2007 1148 1161
    • (2007) Cell. Microbiol. , vol.9 , pp. 1148-1161
    • Moese, S.1    Selbach, M.2    Meyer, T.F.3
  • 20
    • 4344573494 scopus 로고    scopus 로고
    • The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading
    • Z. Zhang, and G. Izaguirre B. Haimovich The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading Mol. Biol. Cell 15 2004 4234 4247
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4234-4247
    • Zhang, Z.1    Izaguirre, G.2    Haimovich, B.3
  • 21
    • 0036510387 scopus 로고    scopus 로고
    • A lipid-regulated docking site on vinculin for protein kinase C
    • W.H. Ziegler, and U. Tigges B.M. Jockusch A lipid-regulated docking site on vinculin for protein kinase C J. Biol. Chem. 277 2002 7396 7404
    • (2002) J. Biol. Chem. , vol.277 , pp. 7396-7404
    • Ziegler, W.H.1    Tigges, U.2    Jockusch, B.M.3
  • 22
    • 2442606429 scopus 로고    scopus 로고
    • Vinculin modulation of paxillin-FAK interactions regulates ERK to control survival and motility
    • M.C. Subauste, and O. Pertz K.M. Hahn Vinculin modulation of paxillin-FAK interactions regulates ERK to control survival and motility J. Cell Biol. 165 2004 371 381
    • (2004) J. Cell Biol. , vol.165 , pp. 371-381
    • Subauste, M.C.1    Pertz, O.2    Hahn, K.M.3
  • 23
    • 0031817205 scopus 로고    scopus 로고
    • Differences in elasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy
    • W.H. Goldmann, and R. Galneder R.M. Ezzell Differences in elasticity of vinculin-deficient F9 cells measured by magnetometry and atomic force microscopy Exp. Cell Res. 239 1998 235 242
    • (1998) Exp. Cell Res. , vol.239 , pp. 235-242
    • Goldmann, W.H.1    Galneder, R.2    Ezzell, R.M.3
  • 24
    • 66749149377 scopus 로고    scopus 로고
    • Becoming stable and strong: The interplay between vinculin exchange dynamics and adhesion strength during adhesion site maturation
    • C. Möhl, and N. Kirchgessner B. Hoffmann Becoming stable and strong: the interplay between vinculin exchange dynamics and adhesion strength during adhesion site maturation Cell Motil. Cytoskeleton 66 2009 350 364
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 350-364
    • Möhl, C.1    Kirchgessner, N.2    Hoffmann, B.3
  • 25
    • 77956268219 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of vinculin at position 1065 modifies focal adhesion dynamics and cell tractions
    • K. Küpper, and N. Lang B. Hoffmann Tyrosine phosphorylation of vinculin at position 1065 modifies focal adhesion dynamics and cell tractions Biochem. Biophys. Res. Commun. 399 2010 560 564
    • (2010) Biochem. Biophys. Res. Commun. , vol.399 , pp. 560-564
    • Küpper, K.1    Lang, N.2    Hoffmann, B.3
  • 26
    • 73449093847 scopus 로고    scopus 로고
    • Anchorage of vinculin to lipid membranes influences cell mechanical properties
    • G. Diez, and P. Kollmannsberger W.H. Goldmann Anchorage of vinculin to lipid membranes influences cell mechanical properties Biophys. J. 97 2009 3105 3112
    • (2009) Biophys. J. , vol.97 , pp. 3105-3112
    • Diez, G.1    Kollmannsberger, P.2    Goldmann, W.H.3
  • 27
    • 77955266643 scopus 로고    scopus 로고
    • Vinculin's C-terminal region facilitates phospholipid membrane insertion
    • V.F. Wirth, and F. List W.H. Goldmann Vinculin's C-terminal region facilitates phospholipid membrane insertion Biochem. Biophys. Res. Commun. 398 2010 433 437
    • (2010) Biochem. Biophys. Res. Commun. , vol.398 , pp. 433-437
    • Wirth, V.F.1    List, F.2    Goldmann, W.H.3
  • 28
    • 0027373782 scopus 로고
    • Activation of protein kinase C precedes alpha 5 beta 1 integrin-mediated cell spreading on fibronectin
    • K. Vuori, and E. Ruoslahti Activation of protein kinase C precedes alpha 5 beta 1 integrin-mediated cell spreading on fibronectin J. Biol. Chem. 268 1993 21459 21462
    • (1993) J. Biol. Chem. , vol.268 , pp. 21459-21462
    • Vuori, K.1    Ruoslahti, E.2
  • 29
    • 0026562948 scopus 로고
    • Glycogen phosphorylase: Control by phosphorylation and allosteric effectors
    • L.N. Johnson Glycogen phosphorylase: control by phosphorylation and allosteric effectors FASEB J. 6 1992 2274 2282
    • (1992) FASEB J. , vol.6 , pp. 2274-2282
    • Johnson, L.N.1
  • 30
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases; Controlling activity through activation segment conformation
    • B. Nolen, S. Taylor, and G. Ghosh Regulation of protein kinases; controlling activity through activation segment conformation Mol. Cell 15 2004 661 675
    • (2004) Mol. Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 31
    • 0029860548 scopus 로고    scopus 로고
    • Structural characterization of the phosphotyrosine binding region of a high-affinity SH2 domain-phosphopeptide complex by molecular dynamics simulation and chemical shift calculations
    • M. Feng, and M. Phillippopoulos C. Lim Structural characterization of the phosphotyrosine binding region of a high-affinity SH2 domain-phosphopeptide complex by molecular dynamics simulation and chemical shift calculations J. Am. Chem. Soc. 118 1996 11265 11277
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11265-11277
    • Feng, M.1    Phillippopoulos, M.2    Lim, C.3
  • 32
    • 0026793591 scopus 로고
    • Inhibition of SH2 domain/phosphoprotein association by a nonhydrolyzable phosphonopeptide
    • S.M. Domchek, and K.R. Auger S.E. Shoelson Inhibition of SH2 domain/phosphoprotein association by a nonhydrolyzable phosphonopeptide Biochemistry 31 1992 9865 9870
    • (1992) Biochemistry , vol.31 , pp. 9865-9870
    • Domchek, S.M.1    Auger, K.R.2    Shoelson, S.E.3
  • 33
    • 18844383462 scopus 로고    scopus 로고
    • A phosphoserine-lysine salt bridge within an alpha-helical peptide, the strongest alpha-helix side-chain interaction measured to date
    • N. Errington, and A.J. Doig A phosphoserine-lysine salt bridge within an alpha-helical peptide, the strongest alpha-helix side-chain interaction measured to date Biochemistry 44 2005 7553 7558
    • (2005) Biochemistry , vol.44 , pp. 7553-7558
    • Errington, N.1    Doig, A.J.2
  • 34
    • 3242875461 scopus 로고    scopus 로고
    • Structural basis for vinculin activation at sites of cell adhesion
    • C. Bakolitsa, and D.M. Cohen R.C. Liddington Structural basis for vinculin activation at sites of cell adhesion Nature 430 2004 583 586
    • (2004) Nature , vol.430 , pp. 583-586
    • Bakolitsa, C.1    Cohen, D.M.2    Liddington, R.C.3
  • 35
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • K. Arnold, and L. Bordoli T. Schwede The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling Bioinformatics 22 2006 195 201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Schwede, T.3
  • 37
    • 0041784950 scopus 로고    scopus 로고
    • All-atom empirical potential for molecular modeling and dynamics studies of proteins
    • A. MacKerell, and D. Bashford M. Karplus All-atom empirical potential for molecular modeling and dynamics studies of proteins J. Phys. Chem. B 102 1998 3586 3616
    • (1998) J. Phys. Chem. B , vol.102 , pp. 3586-3616
    • MacKerell, A.1    Bashford, D.2    Karplus, M.3
  • 38
    • 4444351490 scopus 로고    scopus 로고
    • Empirical force fields for biological macromolecules: Overview and issues
    • A.D. Mackerell Jr. Empirical force fields for biological macromolecules: overview and issues J. Comput. Chem. 25 2004 1584 1604
    • (2004) J. Comput. Chem. , vol.25 , pp. 1584-1604
    • MacKerell, Jr.A.D.1
  • 39
    • 0035871686 scopus 로고    scopus 로고
    • A fast SHAKE algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations
    • V. Kräutler, W.F.van Gunsteren, and P.H. Hünenberger A fast SHAKE algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations J. Comput. Chem. 22 2001 501 508
    • (2001) J. Comput. Chem. , vol.22 , pp. 501-508
    • Kräutler, V.1    Gunsteren, W.F.V.2    Hünenberger, P.H.3
  • 40
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • W.G. Hoover Canonical dynamics: equilibrium phase-space distributions Phys. Rev. A 31 1985 1695 1697
    • (1985) Phys. Rev. A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 41
    • 65449131260 scopus 로고    scopus 로고
    • Lipid binding to the tail domain of vinculin: Specificity and the role of the N and C termini
    • S.M. Palmer, and M.P. Playford S.L. Campbell Lipid binding to the tail domain of vinculin: specificity and the role of the N and C termini J. Biol. Chem. 284 2009 7223 7231
    • (2009) J. Biol. Chem. , vol.284 , pp. 7223-7231
    • Palmer, S.M.1    Playford, M.P.2    Campbell, S.L.3
  • 42
    • 0038675609 scopus 로고    scopus 로고
    • Effective energy function for proteins in lipid membranes
    • T. Lazaridis Effective energy function for proteins in lipid membranes Proteins 52 2003 176 192
    • (2003) Proteins , vol.52 , pp. 176-192
    • Lazaridis, T.1
  • 43
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • W.L. Jorgensen, and J. Chandrasekhar M.L. Klein Comparison of simple potential functions for simulating liquid water J. Chem. Phys. 79 1983 926 935
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Klein, M.L.3
  • 44
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • A.A. Russo, P.D. Jeffrey, and N.P. Pavletich Structural basis of cyclin-dependent kinase activation by phosphorylation Nat. Struct. Biol. 3 1996 696 700
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 45
    • 12844283323 scopus 로고    scopus 로고
    • The SH2 domain: Versatile signaling module and pharmaceutical target
    • K. Machida, and B.J. Mayer The SH2 domain: versatile signaling module and pharmaceutical target Biochim. Biophys. Acta 1747 2005 1 25
    • (2005) Biochim. Biophys. Acta , vol.1747 , pp. 1-25
    • MacHida, K.1    Mayer, B.J.2
  • 46
    • 67049146466 scopus 로고    scopus 로고
    • Molecular mechanics of the alpha-actinin rod domain: Bending, torsional, and extensional behavior
    • J. Golji, R. Collins, and M.R. Mofrad Molecular mechanics of the alpha-actinin rod domain: bending, torsional, and extensional behavior PLOS Comput. Biol. 5 2009 e1000389
    • (2009) PLOS Comput. Biol. , vol.5 , pp. 1000389
    • Golji, J.1    Collins, R.2    Mofrad, M.R.3
  • 47
    • 77954486800 scopus 로고    scopus 로고
    • Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics
    • C. Grashoff, and B.D. Hoffman M.A. Schwartz Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics Nature 466 2010 263 266
    • (2010) Nature , vol.466 , pp. 263-266
    • Grashoff, C.1    Hoffman, B.D.2    Schwartz, M.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.