메뉴 건너뛰기




Volumn 85, Issue 6, 2006, Pages 487-500

Role of vinculin in regulating focal adhesion turnover

Author keywords

Cell motility; Focal adhesions; Interference reflection microscopy; PIP2; Talin; Vinculin

Indexed keywords

F ACTIN; GREEN FLUORESCENT PROTEIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; VINCULIN;

EID: 33646552096     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2006.01.014     Document Type: Article
Times cited : (153)

References (51)
  • 4
    • 0029761645 scopus 로고    scopus 로고
    • The focal adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin
    • Brindle N.P.J., Holt M.R., Davies J.E., Price C.J., and Critchley D.R. The focal adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the proline-rich domain in vinculin. Biochem. J. 318 (1996) 753-757
    • (1996) Biochem. J. , vol.318 , pp. 753-757
    • Brindle, N.P.J.1    Holt, M.R.2    Davies, J.E.3    Price, C.J.4    Critchley, D.R.5
  • 7
    • 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. Spatial distribution and functional significance of activated vinculin in living cells. J. Cell Biol. 169 (2005) 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
    • 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. Recruitment of the Arp2/3 complex to vinculin, coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159 (2002) 881-891
    • (2002) J. Cell Biol. , vol.159 , pp. 881-891
    • DeMali, K.A.1    Barlow, C.A.2    Burridge, K.3
  • 11
    • 1842584776 scopus 로고    scopus 로고
    • Newest findings on the oldest oncogene: how activated src does it
    • Frame M.C. Newest findings on the oldest oncogene: how activated src does it. J. Cell Sci. 117 (2004) 989-998
    • (2004) J. Cell Sci. , vol.117 , pp. 989-998
    • Frame, M.C.1
  • 12
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith C.G., Yamada K.M., and Sheetz M.P. 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
  • 13
    • 0242361579 scopus 로고    scopus 로고
    • Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation
    • Giannone G., Jiang G., Sutton D.H., Critchley D.R., and Sheetz M.P. Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation. J. Cell Biol. 163 (2003) 409-419
    • (2003) J. Cell Biol. , vol.163 , pp. 409-419
    • Giannone, G.1    Jiang, G.2    Sutton, D.H.3    Critchley, D.R.4    Sheetz, M.P.5
  • 14
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate
    • Gilmore A.P., and Burridge K. Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate. Nature 381 (1996) 531-535
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 15
    • 0036293439 scopus 로고    scopus 로고
    • Intact vinculin protein is required for control of cell shape, cell mechanics, and rac-dependent lamellipodia formation
    • Goldmann W.H., and Ingber D.E. Intact vinculin protein is required for control of cell shape, cell mechanics, and rac-dependent lamellipodia formation. Biochem. Biophys. Res. Commun. 290 (2002) 749-755
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 749-755
    • Goldmann, W.H.1    Ingber, D.E.2
  • 16
    • 0034618121 scopus 로고    scopus 로고
    • Restructuring of focal adhesion plaques by PI 3-kinase, regulation by PtdIns (3,4,5)-P3 binding to α-actinin
    • Greenwood J.A., Thiebert A.B., Prestwich G.D., and Murphy-Ulrich J.E. Restructuring of focal adhesion plaques by PI 3-kinase, regulation by PtdIns (3,4,5)-P3 binding to α-actinin. J. Cell Biol. 150 (2000) 627-641
    • (2000) J. Cell Biol. , vol.150 , pp. 627-641
    • Greenwood, J.A.1    Thiebert, A.B.2    Prestwich, G.D.3    Murphy-Ulrich, J.E.4
  • 17
    • 0027787894 scopus 로고
    • The importance of not saturating H2O in protein NMR. Application to sensitivity enhancement and NOE measurements
    • Grzesiek S., and Bax A. The importance of not saturating H2O in protein NMR. Application to sensitivity enhancement and NOE measurements. J. Am. Chem. Soc. 115 (1993) 12593-12594
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12593-12594
    • Grzesiek, S.1    Bax, A.2
  • 18
    • 0032559997 scopus 로고    scopus 로고
    • The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate
    • Huttelmaier S., Mayboroda O., Harbeck B., Jarchau T., Jockusch B.M., and Rudiger M. The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate. Curr. Biol. 8 (1998) 479-488
    • (1998) Curr. Biol. , vol.8 , pp. 479-488
    • Huttelmaier, S.1    Mayboroda, O.2    Harbeck, B.3    Jarchau, T.4    Jockusch, B.M.5    Rudiger, M.6
  • 20
    • 0031044781 scopus 로고    scopus 로고
    • Focal adhesion kinase, at the crossroads of signal transduction
    • Ilic D., Damsky C.H., and Yamamoto T. Focal adhesion kinase, at the crossroads of signal transduction. J. Cell Sci. 110 (1997) 401-407
    • (1997) J. Cell Sci. , vol.110 , pp. 401-407
    • Ilic, D.1    Damsky, C.H.2    Yamamoto, T.3
  • 21
    • 0041461882 scopus 로고    scopus 로고
    • Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin
    • Jiang G., Giannone G., Critchley D.R., Fukumoto E., and Sheetz M.P. Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 424 (2003) 334-337
    • (2003) Nature , vol.424 , pp. 334-337
    • Jiang, G.1    Giannone, G.2    Critchley, D.R.3    Fukumoto, E.4    Sheetz, M.P.5
  • 22
    • 0030222341 scopus 로고    scopus 로고
    • Crosstalk between cell adhesion molecules, vinculin as a paradigm for regulation by conformation
    • Jockusch B.M., and Rudiger M. Crosstalk between cell adhesion molecules, vinculin as a paradigm for regulation by conformation. Trends Cell Biol. 6 (1996) 311-315
    • (1996) Trends Cell Biol. , vol.6 , pp. 311-315
    • Jockusch, B.M.1    Rudiger, M.2
  • 23
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson R.P., and Craig S.W. An intramolecular association between the head and tail domains of vinculin modulates talin binding. J. Biol. Chem. 269 (1994) 12611-12619
    • (1994) J. Biol. Chem. , vol.269 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 24
    • 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. F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature 373 (1995) 261-264
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 25
    • 0034614610 scopus 로고    scopus 로고
    • Actin activates a cryptic dimerisation potential of the vinculin tail domain
    • Johnson R.P., and Craig S.W. Actin activates a cryptic dimerisation potential of the vinculin tail domain. J. Biol. Chem. 275 (2000) 95-105
    • (2000) J. Biol. Chem. , vol.275 , pp. 95-105
    • Johnson, R.P.1    Craig, S.W.2
  • 26
    • 0032516467 scopus 로고    scopus 로고
    • A conserved motif in the tail domain of vinculin mediates association with and insertion into acidic phospholipid bilayers
    • Johnson R.P., Niggli V., Durrer P., and Craig S.W. A conserved motif in the tail domain of vinculin mediates association with and insertion into acidic phospholipid bilayers. Biochemistry 37 (1998) 10211-10222
    • (1998) Biochemistry , vol.37 , pp. 10211-10222
    • Johnson, R.P.1    Niggli, V.2    Durrer, P.3    Craig, S.W.4
  • 29
    • 0037038412 scopus 로고    scopus 로고
    • Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions
    • Ling K., Doughman R.L., Firestone A.J., Bunce M.W., and Anderson R.A. Type I gamma phosphatidylinositol phosphate kinase targets and regulates focal adhesions. Nature 420 (2002) 89-93
    • (2002) Nature , vol.420 , pp. 89-93
    • Ling, K.1    Doughman, R.L.2    Firestone, A.J.3    Bunce, M.W.4    Anderson, R.A.5
  • 31
    • 0034121267 scopus 로고    scopus 로고
    • Talin controls the exit of the integrin α5β1 from an early compartment of the secretory pathway
    • Martel V., Vignoud L., Dupe S., Frachet P., Block M.R., and Albiges-Rizo C. Talin controls the exit of the integrin α5β1 from an early compartment of the secretory pathway. J. Cell Sci. 113 (2000) 1951-1961
    • (2000) J. Cell Sci. , vol.113 , pp. 1951-1961
    • Martel, V.1    Vignoud, L.2    Dupe, S.3    Frachet, P.4    Block, M.R.5    Albiges-Rizo, C.6
  • 32
    • 0034160011 scopus 로고    scopus 로고
    • Integrin signalling, a new Cas(t) of characters enters the stage
    • O'Neill G.M., Fashena S.J., and Golemis E.A. Integrin signalling, a new Cas(t) of characters enters the stage. Trends Cell Biol. 10 (2000) 111-119
    • (2000) Trends Cell Biol. , vol.10 , pp. 111-119
    • O'Neill, G.M.1    Fashena, S.J.2    Golemis, E.A.3
  • 33
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous solutions
    • Piotto M., Saudek V., and Sklenar V. Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous solutions. J. Biol. NMR 2 (1992) 661-665
    • (1992) J. Biol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 34
    • 0033695362 scopus 로고    scopus 로고
    • Structure of the dimerisation and β-catenin-binding region of α-catenin
    • Pokutta S., and Weis W.L. Structure of the dimerisation and β-catenin-binding region of α-catenin. Mol. Cell 5 (2000) 533-543
    • (2000) Mol. Cell , vol.5 , pp. 533-543
    • Pokutta, S.1    Weis, W.L.2
  • 35
  • 36
    • 0034695461 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion
    • Raucher D., Stauffer T., Chen W., Shen K., Guo S., York J.D., Sheetz M.P., and Meyer T. Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion. Cell 100 (2000) 221-228
    • (2000) Cell , vol.100 , pp. 221-228
    • Raucher, D.1    Stauffer, T.2    Chen, W.3    Shen, K.4    Guo, S.5    York, J.D.6    Sheetz, M.P.7    Meyer, T.8
  • 39
    • 0027326435 scopus 로고
    • Suppression of vinculin expression by antisense transfection confers changes in cell morphology, motility, and anchorage-dependent growth of 3T3 cells
    • Rodriguez Fernandez J.L., Geiger B., Salomon D., and Ben'Zeev A. Suppression of vinculin expression by antisense transfection confers changes in cell morphology, motility, and anchorage-dependent growth of 3T3 cells. J. Cell Biol. 122 (1993) 1285-1294
    • (1993) J. Cell Biol. , vol.122 , pp. 1285-1294
    • Rodriguez Fernandez, J.L.1    Geiger, B.2    Salomon, D.3    Ben'Zeev, A.4
  • 40
    • 0033603360 scopus 로고    scopus 로고
    • Polyphosphoinositides inhibit the interaction of vinculin with actin filaments
    • Steimle P.A., Hoffert J.D., Adey N.B., and Craig S.W. Polyphosphoinositides inhibit the interaction of vinculin with actin filaments. J. Biol. Chem. 274 (1999) 18414-18420
    • (1999) J. Biol. Chem. , vol.274 , pp. 18414-18420
    • Steimle, P.A.1    Hoffert, J.D.2    Adey, N.B.3    Craig, S.W.4
  • 41
    • 2442606429 scopus 로고    scopus 로고
    • Vinculin modulation of paxillin-FAK interactions regulates ERK to control survival and motility
    • Subauste M.C., Pertz O., Adamson E.D., Turner C.E., Junger S., and Hahn K.M. 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    Adamson, E.D.3    Turner, C.E.4    Junger, S.5    Hahn, K.M.6
  • 42
    • 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. Vinexin beta regulates the anchorage dependence of ERK2 activation stimulated by epidermal growth factor. J. Biol. Chem. 277 (2002) 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
  • 44
    • 0033666291 scopus 로고    scopus 로고
    • Paxillin and focal adhesion signalling
    • Turner C.E. Paxillin and focal adhesion signalling. Nat. Cell Biol. 2 (2000) E231-E236
    • (2000) Nat. Cell Biol. , vol.2
    • Turner, C.E.1
  • 47
    • 0029918344 scopus 로고    scopus 로고
    • Acidic phospholipids inhibit the intramolecular association between the N- and C-terminal regions of vinculin, exposing actin-binding and protein kinase C phosphorylation sites
    • Weekes J., Barry S.T., and Critchley D.R. Acidic phospholipids inhibit the intramolecular association between the N- and C-terminal regions of vinculin, exposing actin-binding and protein kinase C phosphorylation sites. Biochem. J. 314 (1996) 827-832
    • (1996) Biochem. J. , vol.314 , pp. 827-832
    • Weekes, J.1    Barry, S.T.2    Critchley, D.R.3
  • 48
    • 0028324634 scopus 로고
    • Characterisation of the paxillin-binding site and the C-terminal focal adhesion targeting sequence in vinculin
    • Wood C.K., Turner C.E., Jackson P., and Critchley D.R. Characterisation of the paxillin-binding site and the C-terminal focal adhesion targeting sequence in vinculin. J. Cell Sci. 107 (1994) 709-717
    • (1994) J. Cell Sci. , vol.107 , pp. 709-717
    • Wood, C.K.1    Turner, C.E.2    Jackson, P.3    Critchley, D.R.4
  • 49
    • 0031836593 scopus 로고    scopus 로고
    • Rescue of the mutant phenotype by reexpression of full-length vinculin in null F9 cells: effects on cell locomotion by domain deleted vinculin
    • Xu W., Coll J.-L., and Adamson E.D. Rescue of the mutant phenotype by reexpression of full-length vinculin in null F9 cells: effects on cell locomotion by domain deleted vinculin. J. Cell Sci. 111 (1998) 1535-1544
    • (1998) J. Cell Sci. , vol.111 , pp. 1535-1544
    • Xu, W.1    Coll, J.-L.2    Adamson, E.D.3
  • 50
    • 0031929760 scopus 로고    scopus 로고
    • Vinculin knockout results in heart and brain defects during embryonic development
    • Xu W., Baribault H., and Adamson E.D. Vinculin knockout results in heart and brain defects during embryonic development. Development 125 (1998) 327-337
    • (1998) Development , vol.125 , pp. 327-337
    • Xu, W.1    Baribault, H.2    Adamson, E.D.3
  • 51
    • 0036510387 scopus 로고    scopus 로고
    • A lipid-regulated docking site on vinculin for protein kinase C
    • Ziegler W.H., Tigges U., Zieseniss A., and Jockusch B.M. 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    Zieseniss, A.3    Jockusch, B.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.