메뉴 건너뛰기




Volumn 430, Issue 6999, 2004, Pages 583-586

Structural basis for vinculin activation at sites of cell adhesion

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION; AMINO ACIDS; CRYSTAL STRUCTURE; MOLECULES; PROTEINS; THERMODYNAMICS;

EID: 3242875461     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02610     Document Type: Article
Times cited : (314)

References (30)
  • 1
    • 0029034976 scopus 로고
    • Focal adhesion formation by F9 embryonal carcinoma cells after vinculin gene disruption
    • Volberg, T. et al. Focal adhesion formation by F9 embryonal carcinoma cells after vinculin gene disruption. J. Cell Sci. 108, 2253-2260 (1995).
    • (1995) J. Cell Sci. , vol.108 , pp. 2253-2260
    • Volberg, T.1
  • 2
    • 0031929760 scopus 로고    scopus 로고
    • Vinculin knockout results in heart and brain defects during embryonic development
    • Xu, W. M., Biribault, H. & Adamson, E. D. Vinculin knockout results in heart and brain defects during embryonic development. Development 125, 327-337 (1998).
    • (1998) Development , vol.125 , pp. 327-337
    • Xu, W.M.1    Biribault, H.2    Adamson, E.D.3
  • 3
    • 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. & Burridge, K. Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell Biol. 159, 881-891 (2002).
    • (2002) J. Cell Biol. , vol.159 , pp. 881-891
    • DeMali, K.A.1    Barlow, C.A.2    Burridge, K.3
  • 4
    • 0028318397 scopus 로고
    • An Intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson, R. P. & Craig, S. W. An Intramolecular association between the head and tail domains of vinculin modulates talin binding. J. Biol. Chem. 269, 12611-12619 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 5
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • Johnson, R. P. & Craig, S.W. F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature 373, 261-264 (1995).
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 6
    • 0343058961 scopus 로고    scopus 로고
    • The ultrastructure of chicken gizzard vinculin as visualised by high-resolution electron microscopy
    • Winkler, J., Lunsdorf, H. & Jockusch, B. M. The ultrastructure of chicken gizzard vinculin as visualised by high-resolution electron microscopy. J. Struct. Biol. 116, 270-277 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 270-277
    • Winkler, J.1    Lunsdorf, H.2    Jockusch, B.M.3
  • 7
  • 8
    • 0035898657 scopus 로고    scopus 로고
    • Crystal structure of the M-fragment of α-catenin: Implications for modulation of cell adhesion
    • Yang, J., Dokurno, P., Tonks, N. K. & Barford, D. Crystal structure of the M-fragment of α-catenin: implications for modulation of cell adhesion. EMBO J. 20, 3645-3656. (2001).
    • (2001) EMBO J. , vol.20 , pp. 3645-3656
    • Yang, J.1    Dokurno, P.2    Tonks, N.K.3    Barford, D.4
  • 9
    • 0347717894 scopus 로고    scopus 로고
    • Vinculin activation by talin through helical bundle conversion
    • Izard, T. et al. Vinculin activation by talin through helical bundle conversion. Nature 427, 171-175 (2004).
    • (2004) Nature , vol.427 , pp. 171-175
    • Izard, T.1
  • 10
    • 0037166245 scopus 로고    scopus 로고
    • Biochemical and structural definition of the 1-afadin- and actin-binding sites of α-catenin
    • Pokutta, S., Drees, F., Takai, Y., Nelson, W. J. & Weis, W. I. Biochemical and structural definition of the 1-afadin- and actin-binding sites of α-catenin. J. Biol. Chem. 277, 18868-18874 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 18868-18874
    • Pokutta, S.1    Drees, F.2    Takai, Y.3    Nelson, W.J.4    Weis, W.I.5
  • 11
    • 0033695362 scopus 로고    scopus 로고
    • Structure of the dimerization and β-catenin-binding region of α-catenin
    • Pokutta, S. & Weis, W. I. Structure of the dimerization and β-catenin-binding region of α-catenin. Mol. Cell 5, 533-543 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 533-543
    • Pokutta, S.1    Weis, W.I.2
  • 12
    • 0035800738 scopus 로고    scopus 로고
    • Conformational change in the vinculin C-terminal depends on a critical histidine residue (His-906)
    • Miller, G. J. & Ball, E. H. Conformational change in the vinculin C-terminal depends on a critical histidine residue (His-906). J. Biol. Chem. 276, 28829-28834 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 28829-28834
    • Miller, G.J.1    Ball, E.H.2
  • 13
    • 0029761645 scopus 로고    scopus 로고
    • The focal adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the prolin-rich domain in vinculin
    • Brindle, N. P. J., Holt, M. R., Davies, J. E., Price, C. J. & Critchley, D. R. The focal adhesion vasodilator-stimulated phosphoprotein (VASP) binds to the prolin-rich domain in vinculin. Biochem. J. 318, 753-757 (1996).
    • (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
  • 14
    • 0033545092 scopus 로고    scopus 로고
    • Vinexin: A novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organisation
    • Kioka, N. et al. Vinexin: a novel vinculin-binding protein with multiple SH3 domains enhances actin cytoskeletal organisation. J. Cell Biol. 144, 59-69 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 59-69
    • Kioka, N.1
  • 15
    • 0032559997 scopus 로고    scopus 로고
    • The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate
    • Huttelmaier, S. et al. The interaction of the cell-contact proteins VASP and vinculin is regulated by phosphatidylinositol-4,5-bisphosphate. Curr. Biol. 8, 479-488 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 479-488
    • Huttelmaier, S.1
  • 16
    • 0024542932 scopus 로고
    • Primary sequence and domain-structure of chicken vinculin
    • Price, G. J. et al. Primary sequence and domain-structure of chicken vinculin. Biochem. J. 259, 453-461 (1989).
    • (1989) Biochem. J. , vol.259 , pp. 453-461
    • Price, G.J.1
  • 17
    • 0037086555 scopus 로고    scopus 로고
    • Further characterization of the interaction between the cytoskeletal proteins talin and vinculin
    • Bass, M. D. et al. Further characterization of the interaction between the cytoskeletal proteins talin and vinculin. Biochem. J. 362, 761-768 (2002).
    • (2002) Biochem. J. , vol.362 , pp. 761-768
    • Bass, M.D.1
  • 18
    • 0033594088 scopus 로고    scopus 로고
    • Functional domains of α-catenin required for the strong state of cadherin-based cell adhesion
    • Imamura, Y., Itoh, M., Maeno, Y., Tsukita, S. & Nagafuchi, A. Functional domains of α-catenin required for the strong state of cadherin-based cell adhesion. J. Cell Biol. 144, 1311-1322 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 1311-1322
    • Imamura, Y.1    Itoh, M.2    Maeno, Y.3    Tsukita, S.4    Nagafuchi, A.5
  • 19
    • 0030956869 scopus 로고    scopus 로고
    • Isolation of peptides from phage-displayed random peptide libraries that interact with the talin-binding domain of vinculin
    • Adey, N. B. & Kay, B. K. Isolation of peptides from phage-displayed random peptide libraries that interact with the talin-binding domain of vinculin. Biochem. J. 324, 523-528 (1997).
    • (1997) Biochem. J. , vol.324 , pp. 523-528
    • Adey, N.B.1    Kay, B.K.2
  • 20
    • 0033603360 scopus 로고    scopus 로고
    • Polyphosphoinositides inhibit the interaction of vinculin with actin filaments
    • Steimle, P. A., Hoffert, J. D., Adey, N. B. & Craig, S. W. Polyphosphoinositides inhibit the interaction of vinculin with actin filaments. J. Biol. Chem. 274, 18414-18420 (1999).
    • (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
  • 21
    • 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. & Craig, S. W. A conserved motif in the tail domain of vinculin mediates association with and insertion into acidic phospholipid bilayers. Biochemistry 37, 10211-10222 (1998).
    • (1998) Biochemistry , vol.37 , pp. 10211-10222
    • Johnson, R.P.1    Niggli, V.2    Durrer, P.3    Craig, S.W.4
  • 22
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate
    • Gilmore, A. P. & Burridge, K. Regulation of vinculin binding to talin and actin by phosphatidylinositol-4-5-bisphosphate. Nature 381, 531-535 (1996).
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 23
    • 3242877264 scopus 로고    scopus 로고
    • Three-dimensional structure of vinculin bound to actin filaments
    • submitted
    • Janssen, M. E. W. et al. Three-dimensional structure of vinculin bound to actin filaments. J. Cell Biol. (submitted).
    • J. Cell Biol.
    • Janssen, M.E.W.1
  • 24
    • 0034715924 scopus 로고    scopus 로고
    • The structural basis of dynamic cell adhesion: Heads, tails and allostery
    • Liddington, R. C. & Bankston, L. A. The structural basis of dynamic cell adhesion: heads, tails and allostery. Exp. Cell Res. 261, 37-43 (2000).
    • (2000) Exp. Cell Res. , vol.261 , pp. 37-43
    • Liddington, R.C.1    Bankston, L.A.2
  • 25
    • 0036468436 scopus 로고    scopus 로고
    • The modular logic of signaling proteins: Building allosteric switches from simple binding domains
    • Lim, W. A. The modular logic of signaling proteins: building allosteric switches from simple binding domains. Curr. Opin. Struct. Biol. 12, 61-68 (2002).
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 61-68
    • Lim, W.A.1
  • 26
    • 0035976972 scopus 로고    scopus 로고
    • Localization of an integrin binding site to the C terminus of talin
    • Xing, B., Jedsadayanmata, A. & Lam, S. C. Localization of an integrin binding site to the C terminus of talin. J. Biol. Chem. 276, 44373-44378 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 44373-44378
    • Xing, B.1    Jedsadayanmata, A.2    Lam, S.C.3
  • 27
    • 0022958824 scopus 로고
    • Purification and assay of vinculin, metavinculin, and talin
    • O'Halloran, T., Molony, L. & Burridge, K. Purification and assay of vinculin, metavinculin, and talin. Methods Enzymol. 134, 69-77 (1986).
    • (1986) Methods Enzymol. , vol.134 , pp. 69-77
    • O'Halloran, T.1    Molony, L.2    Burridge, K.3
  • 28
    • 0038210935 scopus 로고    scopus 로고
    • Advances in direct methods for protein crystallography
    • Uson, I. & Sheldrick, G. M. Advances in direct methods for protein crystallography. Curr. Opin. Struct. Biol. 9, 642-648 (1999),
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 642-648
    • Uson, I.1    Sheldrick, G.M.2
  • 29
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de la Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997),
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 30
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.