메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

Vinculin controls talin engagement with the actomyosin machinery

Author keywords

[No Author keywords available]

Indexed keywords

MYOSIN ADENOSINE TRIPHOSPHATASE; TALIN; VINCULIN; ACTIN; PROTEIN BINDING;

EID: 84949310075     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms10038     Document Type: Article
Times cited : (158)

References (64)
  • 1
    • 84867872264 scopus 로고    scopus 로고
    • Assembly and disassembly of cell matrix adhesions
    • Wehrle-Haller, B. Assembly and disassembly of cell matrix adhesions. Curr. Opin. Cell. Biol. 24, 569-581 (2012).
    • (2012) Curr. Opin. Cell. Biol. , vol.24 , pp. 569-581
    • Wehrle-Haller, B.1
  • 3
    • 84869102195 scopus 로고    scopus 로고
    • Finding the weakest link: Exploring integrin-mediated mechanical molecular pathways
    • Roca-Cusachs, P., Iskratsch, T. & Sheetz, M. P. Finding the weakest link: exploring integrin-mediated mechanical molecular pathways. J. Cell. Sci. 125, 3025-3038 (2012).
    • (2012) J. Cell. Sci. , vol.125 , pp. 3025-3038
    • Roca-Cusachs, P.1    Iskratsch, T.2    Sheetz, M.P.3
  • 4
    • 51049100594 scopus 로고    scopus 로고
    • Talin depletion reveals independence of initial cell spreading from integrin activation and traction
    • Zhang, X. et al. Talin depletion reveals independence of initial cell spreading from integrin activation and traction. Nat. Cell Biol. 10, 1062-1068 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1062-1068
    • Zhang, X.1
  • 5
    • 0029059601 scopus 로고
    • Targeted disruption of vinculin genes in F9 and embryonic stem cells changes cell morphology, adhesion, and locomotion
    • Coll, J. L. et al. Targeted disruption of vinculin genes in F9 and embryonic stem cells changes cell morphology, adhesion, and locomotion. Proc. Natl Acad. Sci. USA 92, 9161-9165 (1995).
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9161-9165
    • Coll, J.L.1
  • 6
    • 33646552096 scopus 로고    scopus 로고
    • Role of vinculin in regulating focal adhesion turnover
    • Saunders, R. M. et al. Role of vinculin in regulating focal adhesion turnover. Eur. J. Cell. Biol. 85, 487-500 (2006).
    • (2006) Eur. J. Cell. Biol. , vol.85 , pp. 487-500
    • Saunders, R.M.1
  • 7
    • 36849069902 scopus 로고    scopus 로고
    • Vinculin controls focal adhesion formation by direct interactions with talin and actin
    • Humphries, J. D. et al. Vinculin controls focal adhesion formation by direct interactions with talin and actin. J. Cell Biol. 179, 1043-1057 (2007).
    • (2007) J. Cell Biol. , vol.179 , pp. 1043-1057
    • Humphries, J.D.1
  • 8
    • 84880642716 scopus 로고    scopus 로고
    • Vinculin-actin interaction couples actin retrograde flow to focal adhesions, but is dispensable for focal adhesion growth
    • Thievessen, I. et al. Vinculin-actin interaction couples actin retrograde flow to focal adhesions, but is dispensable for focal adhesion growth. J. Cell Biol. 202, 163-177 (2013).
    • (2013) J. Cell Biol. , vol.202 , pp. 163-177
    • Thievessen, I.1
  • 10
    • 84875439033 scopus 로고    scopus 로고
    • RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover
    • Goult, B. T. et al. RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover. J. Biol. Chem. 288, 8238-8249 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 8238-8249
    • Goult, B.T.1
  • 11
    • 84877157661 scopus 로고    scopus 로고
    • Two modes of integrin activation form a binary molecular switch in adhesion maturation
    • Lee, H.-S., Anekal, P., Lim, C. J., Liu, C.-C. & Ginsberg, M. H. Two modes of integrin activation form a binary molecular switch in adhesion maturation. Mol. Biol. Cell 24, 1354-1362 (2013).
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1354-1362
    • Lee, H.-S.1    Anekal, P.2    Lim, C.J.3    Liu, C.-C.4    Ginsberg, M.H.5
  • 12
    • 27744527513 scopus 로고    scopus 로고
    • Mapping and consensus sequence identification for multiple vinculin binding sites within the talin rod
    • Gingras, A. R. et al. Mapping and consensus sequence identification for multiple vinculin binding sites within the talin rod. J. Biol. Chem. 280, 37217-37224 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 37217-37224
    • Gingras, A.R.1
  • 13
    • 34447116981 scopus 로고    scopus 로고
    • The integrin binding site 2 (IBS2) in the talin rod domain is essential for linking integrin beta subunits to the cytoskeleton
    • Moes, M. et al. The integrin binding site 2 (IBS2) in the talin rod domain is essential for linking integrin beta subunits to the cytoskeleton. J. Biol. Chem. 282, 17280-17288 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 17280-17288
    • Moes, M.1
  • 14
    • 10544241952 scopus 로고    scopus 로고
    • Talin contains three actin-binding sites each of which is adjacent to a vinculin-binding site
    • Hemmings, L. et al. Talin contains three actin-binding sites each of which is adjacent to a vinculin-binding site. J. Cell Sci. 109, 2715-2726 (1996).
    • (1996) J. Cell Sci. , vol.109 , pp. 2715-2726
    • Hemmings, L.1
  • 16
    • 84874652706 scopus 로고    scopus 로고
    • Vinculin regulates the recruitment and release of core focal adhesion proteins in a force-dependent manner
    • Carisey, A. et al. Vinculin regulates the recruitment and release of core focal adhesion proteins in a force-dependent manner. Curr. Biol. 23, 271-281 (2013).
    • (2013) Curr. Biol. , vol.23 , pp. 271-281
    • Carisey, A.1
  • 17
    • 84878985226 scopus 로고    scopus 로고
    • How vinculin regulates force transmission
    • Dumbauld, D. W. et al. How vinculin regulates force transmission. Proc. Natl Acad. Sci. USA 110, 9788-9793 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9788-9793
    • Dumbauld, D.W.1
  • 18
    • 79151482119 scopus 로고    scopus 로고
    • Vinculin, an adapter protein in control of cell adhesion signalling
    • Carisey, A. & Ballestrem, C. Vinculin, an adapter protein in control of cell adhesion signalling. Eur. J. Cell Biol. 90, 157-163 (2011).
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 157-163
    • Carisey, A.1    Ballestrem, C.2
  • 20
    • 4143083987 scopus 로고    scopus 로고
    • Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle
    • Papagrigoriou, E. et al. Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle. EMBO J. 23, 2942-2951 (2004).
    • (2004) EMBO J. , vol.23 , pp. 2942-2951
    • Papagrigoriou, E.1
  • 21
    • 77956510396 scopus 로고    scopus 로고
    • Central region of talin has a unique fold that binds vinculin and actin
    • Gingras, A. R. et al. Central region of talin has a unique fold that binds vinculin and actin. J. Biol. Chem. 285, 29577-29587 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 29577-29587
    • Gingras, A.R.1
  • 22
    • 38549103141 scopus 로고    scopus 로고
    • The structure of the C-terminal actin-binding domain of talin
    • Gingras, A. R. et al. The structure of the C-terminal actin-binding domain of talin. EMBO J. 27, 458-469 (2008).
    • (2008) EMBO J. , vol.27 , pp. 458-469
    • Gingras, A.R.1
  • 23
    • 59149094538 scopus 로고    scopus 로고
    • Stretching single talin rod molecules activates vinculin binding
    • del Rio, A. et al. Stretching single talin rod molecules activates vinculin binding. Science 323, 638-641 (2009).
    • (2009) Science , vol.323 , pp. 638-641
    • Del Rio, A.1
  • 24
    • 84898467976 scopus 로고    scopus 로고
    • Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation
    • Yao, M. et al. Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation. Sci. Rep. 4, 4610 (2014).
    • (2014) Sci. Rep. , vol.4 , pp. 4610
    • Yao, M.1
  • 25
    • 84898457452 scopus 로고    scopus 로고
    • Actomyosin-dependent formation of the mechanosensitive talin-vinculin complex reinforces actin anchoring
    • Ciobanasu, C., Faivre, B. & Le Clainche, C. Actomyosin-dependent formation of the mechanosensitive talin-vinculin complex reinforces actin anchoring. Nat. Commun. 5, 3095 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 3095
    • Ciobanasu, C.1    Faivre, B.2    Le Clainche, C.3
  • 26
    • 84862788899 scopus 로고    scopus 로고
    • New isoform-specific monoclonal antibodies reveal different sub-cellular localisations for talin1 and talin2
    • Praekelt, U. et al. New isoform-specific monoclonal antibodies reveal different sub-cellular localisations for talin1 and talin2. Eur. J. Cell Biol. 91, 180-191 (2012).
    • (2012) Eur. J. Cell Biol. , vol.91 , pp. 180-191
    • Praekelt, U.1
  • 28
    • 84855737428 scopus 로고    scopus 로고
    • The C terminus of talin links integrins to cell cycle progression
    • Wang, P., Ballestrem, C. & Streuli, C. H. The C terminus of talin links integrins to cell cycle progression. J. Cell. Biol. 195, 499-513 (2011).
    • (2011) J. Cell. Biol. , vol.195 , pp. 499-513
    • Wang, P.1    Ballestrem, C.2    Streuli, C.H.3
  • 29
    • 67649395972 scopus 로고    scopus 로고
    • Control of high affinity interactions in the talin C terminus: How talin domains coordinate protein dynamics in cell adhesions
    • Himmel, M. et al. Control of high affinity interactions in the talin C terminus: how talin domains coordinate protein dynamics in cell adhesions. J. Biol. Chem. 284, 13832-13842 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 13832-13842
    • Himmel, M.1
  • 30
    • 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. & Craig, S. W. Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin. J. Biol. Chem. 280, 17109-17117 (2005).
    • (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
  • 32
    • 84455192508 scopus 로고    scopus 로고
    • The vinculin C-terminal hairpin mediates F-actin bundle formation, focal adhesion and cell mechanical properties
    • Shen, K. et al. The vinculin C-terminal hairpin mediates F-actin bundle formation, focal adhesion and cell mechanical properties. J. Biol. Chem. 286, 45103-45115 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 45103-45115
    • Shen, K.1
  • 33
    • 84921633242 scopus 로고    scopus 로고
    • Vinculin-dependent actin bundling regulates cell migration and traction forces
    • Jannie, K. M. et al. Vinculin-dependent actin bundling regulates cell migration and traction forces. Biochem. J. 465, 383-393 (2014).
    • (2014) Biochem. J. , vol.465 , pp. 383-393
    • Jannie, K.M.1
  • 34
    • 33644959112 scopus 로고    scopus 로고
    • Assembly and mechanosensory function of focal adhesions: Experiments and models
    • Bershadsky, A. D. et al. Assembly and mechanosensory function of focal adhesions: experiments and models. Eur. J. Cell Biol. 85, 165-173 (2005).
    • (2005) Eur. J. Cell Biol. , vol.85 , pp. 165-173
    • Bershadsky, A.D.1
  • 35
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism
    • Riveline, D. et al. Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism. J. Cell Biol. 153, 1175-1186 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1175-1186
    • Riveline, D.1
  • 36
    • 0035945353 scopus 로고    scopus 로고
    • Marching at the front and dragging behind: Differential alphaVbeta3-integrin turnover regulates focal adhesion behavior
    • Ballestrem, C., Hinz, B., Imhof, B. A. & Wehrle-Haller, B. Marching at the front and dragging behind: differential alphaVbeta3-integrin turnover regulates focal adhesion behavior. J. Cell Biol. 155, 1319-1332 (2001).
    • (2001) J. Cell Biol. , vol.155 , pp. 1319-1332
    • Ballestrem, C.1    Hinz, B.2    Imhof, B.A.3    Wehrle-Haller, B.4
  • 37
    • 0344465841 scopus 로고    scopus 로고
    • Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells
    • Zaidel-Bar, R., Ballestrem, C., Kam, Z. & Geiger, B. Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells. J. Cell Sci. 116, 4605-4613 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 38
    • 0141865705 scopus 로고    scopus 로고
    • Talin binding to integrin beta tails: A final common step in integrin activation
    • Tadokoro, S. et al. Talin binding to integrin beta tails: a final common step in integrin activation. Science 302, 103-106 (2003).
    • (2003) Science , vol.302 , pp. 103-106
    • Tadokoro, S.1
  • 39
    • 84867084870 scopus 로고    scopus 로고
    • Integrins b1 and b3 exhibit distinct dynamic nanoscale organizations inside focal adhesions
    • Rossier, O. et al. Integrins b1 and b3 exhibit distinct dynamic nanoscale organizations inside focal adhesions. Nat. Cell Biol. 14, 1057-1067 (2012).
    • (2012) Nat. Cell Biol. , vol.14 , pp. 1057-1067
    • Rossier, O.1
  • 40
    • 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. & Sheetz, M. P. Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation. J. Cell Biol. 163, 409-419 (2003).
    • (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
  • 41
    • 33847159264 scopus 로고    scopus 로고
    • Polymerizing actin fibers position integrins primed to probe for adhesion sites
    • Galbraith, C. G., Yamada, K. M. & Galbraith, J. A. Polymerizing actin fibers position integrins primed to probe for adhesion sites. Science 315, 992-995 (2007).
    • (2007) Science , vol.315 , pp. 992-995
    • Galbraith, C.G.1    Yamada, K.M.2    Galbraith, J.A.3
  • 42
    • 84933177566 scopus 로고    scopus 로고
    • Alternative mechanisms for talin to mediate integrin function
    • Klapholz, B. et al. Alternative mechanisms for talin to mediate integrin function. Curr. Biol. 25, 847-857 (2015).
    • (2015) Curr. Biol. , vol.25 , pp. 847-857
    • Klapholz, B.1
  • 43
    • 84925520191 scopus 로고    scopus 로고
    • Talin dependent mechanosensitivity of cell focal adhesions
    • Yan, J., Yao, M., Goult, B. T. & Sheetz, M. P. Talin dependent mechanosensitivity of cell focal adhesions. Cel. Mol. Bioeng 8, 151-159 (2014).
    • (2014) Cel. Mol. Bioeng , vol.8 , pp. 151-159
    • Yan, J.1    Yao, M.2    Goult, B.T.3    Sheetz, M.P.4
  • 44
    • 84898491914 scopus 로고    scopus 로고
    • Force-dependent vinculin binding to talin in live cells: A crucial step in anchoring the actin cytoskeleton to focal adhesions
    • Hirata, H., Tatsumi, H., Lim, C. T. & Sokabe, M. Force-dependent vinculin binding to talin in live cells: a crucial step in anchoring the actin cytoskeleton to focal adhesions. Am. J. Physiol. Cell Physiol. 306, C607-C620 (2014).
    • (2014) Am. J. Physiol. Cell Physiol. , vol.306 , pp. C607-C620
    • Hirata, H.1    Tatsumi, H.2    Lim, C.T.3    Sokabe, M.4
  • 45
    • 84906314998 scopus 로고    scopus 로고
    • Integrin-associated complexes form hierarchically with variable stoichiometry in nascent adhesions
    • Bachir, A. I. et al. Integrin-associated complexes form hierarchically with variable stoichiometry in nascent adhesions. Curr. Biol. 24, 1845-1853 (2014).
    • (2014) Curr. Biol. , vol.24 , pp. 1845-1853
    • Bachir, A.I.1
  • 46
    • 84884814050 scopus 로고    scopus 로고
    • Structural studies on full-length talin1 reveal a compact auto-inhibited dimer: Implications for talin activation
    • Goult, B. T. et al. Structural studies on full-length talin1 reveal a compact auto-inhibited dimer: implications for talin activation. J. Struct. Biol. 184, 21-32 (2013).
    • (2013) J. Struct. Biol. , vol.184 , pp. 21-32
    • Goult, B.T.1
  • 47
    • 84859991132 scopus 로고    scopus 로고
    • Subcellular Localization of Talin is Regulated by Inter-domain Interactions
    • Banno, A. et al. Subcellular Localization of Talin Is Regulated by Inter-domain Interactions. J. Biol. Chem. 287, 13799-13812 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 13799-13812
    • Banno, A.1
  • 48
    • 84862907595 scopus 로고    scopus 로고
    • Phosphoinositide signaling regulates the exocyst complex and polarized integrin trafficking in directionally migrating cells
    • Thapa, N. et al. Phosphoinositide signaling regulates the exocyst complex and polarized integrin trafficking in directionally migrating cells. Dev. Cell 22, 116-130 (2012).
    • (2012) Dev. Cell , vol.22 , pp. 116-130
    • Thapa, N.1
  • 49
    • 5044241734 scopus 로고    scopus 로고
    • ScienceDirect.com-Developmental cell-RIAM, an Ena/VASP and profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion
    • Lafuente, E. M. et al. ScienceDirect.com-Developmental cell-RIAM, an Ena/VASP and profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion. Dev. Cell 7, 585-595 (2004).
    • (2004) Dev. Cell , vol.7 , pp. 585-595
    • Lafuente, E.M.1
  • 50
    • 0035877656 scopus 로고    scopus 로고
    • Conformation, localization, and integrin binding of talin depend on its interaction with phosphoinositides
    • Martel, V. et al. Conformation, localization, and integrin binding of talin depend on its interaction with phosphoinositides. J. Biol. Chem. 276, 21217-21227 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 21217-21227
    • Martel, V.1
  • 51
    • 0033213922 scopus 로고    scopus 로고
    • The Talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation
    • Calderwood, D. A. et al. The Talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation. J. Biol. Chem. 274, 28071-28074 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 28071-28074
    • Calderwood, D.A.1
  • 52
    • 84863041492 scopus 로고    scopus 로고
    • FAK promotes recruitment of talin to nascent adhesions to control cell motility
    • Lawson, C. et al. FAK promotes recruitment of talin to nascent adhesions to control cell motility. J. Cell Biol. 196, 223-232 (2012).
    • (2012) J. Cell Biol. , vol.196 , pp. 223-232
    • Lawson, C.1
  • 53
    • 84940974858 scopus 로고    scopus 로고
    • Talin determines the nanoscale architecture of focal adhesions
    • Liu, J. et al. Talin determines the nanoscale architecture of focal adhesions. Proc. Natl Acad. Sci. USA 112, E4864-E4873 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , pp. E4864-E4873
    • Liu, J.1
  • 54
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate
    • Gilmore, A. P. & Burridge, K. Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate. Nature 381, 531-535 (1996).
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 55
    • 84964313707 scopus 로고    scopus 로고
    • Lipid binding promotes oligomerization and focal adhesion activity of vinculin
    • Chinthalapudi, K. et al. Lipid binding promotes oligomerization and focal adhesion activity of vinculin. J. Cell Biol. 207, 643-656 (2014).
    • (2014) J. Cell Biol. , vol.207 , pp. 643-656
    • Chinthalapudi, K.1
  • 56
    • 84866418618 scopus 로고    scopus 로고
    • Mice carrying a complete deletion of the talin2 coding sequence are viable and fertile
    • Debrand, E. et al. Mice carrying a complete deletion of the talin2 coding sequence are viable and fertile. Biochem. Biophys. Res. Commun. 426, 190-195 (2012).
    • (2012) Biochem. Biophys. Res. Commun. , vol.426 , pp. 190-195
    • Debrand, E.1
  • 57
    • 0024202673 scopus 로고
    • Characteristics of papillary collecting duct cells in primary culture
    • Husted, R. F., Hayashi, M. & Stokes, J. B. Characteristics of papillary collecting duct cells in primary culture. Am. J. Physiol. Renal Physiol. 255, F1160-F1169 (1988).
    • (1988) Am. J. Physiol. Renal Physiol. , vol.255 , pp. F1160-F1169
    • Husted, R.F.1    Hayashi, M.2    Stokes, J.B.3
  • 59
    • 13244291467 scopus 로고    scopus 로고
    • FRAP analysis of binding: Proper and fitting
    • Sprague, B. L. & McNally, J. G. FRAP analysis of binding: proper and fitting. Trends Cell Biol. 15, 84-91 (2005).
    • (2005) Trends Cell Biol. , vol.15 , pp. 84-91
    • Sprague, B.L.1    McNally, J.G.2
  • 60
    • 84934444361 scopus 로고    scopus 로고
    • Micropatterning cell adhesion on polyacrylamide hydrogels
    • Zhang, J., Guo, W.-H., Rape, A. & Wang, Y.-L. Micropatterning cell adhesion on polyacrylamide hydrogels. Methods Mol. Biol. 1066, 147-156 (2013).
    • (2013) Methods Mol. Biol. , vol.1066 , pp. 147-156
    • Zhang, J.1    Guo, W.-H.2    Rape, A.3    Wang, Y.-L.4
  • 61
    • 0344912596 scopus 로고    scopus 로고
    • Cell locomotion and focal adhesions are regulated by substrate flexibility
    • Pelham, R. J. & Wang, Y. L. Cell locomotion and focal adhesions are regulated by substrate flexibility. Proc. Natl Acad. Sci. USA 94, 13661-13665 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 13661-13665
    • Pelham, R.J.1    Wang, Y.L.2
  • 62
    • 84856740623 scopus 로고    scopus 로고
    • Strength in the periphery: Growth cone biomechanics and substrate rigidity response in peripheral and central nervous system neurons
    • Koch, D., Rosoff, W. J., Jiang, J., Geller, H. M. & Urbach, J. S. Strength in the periphery: growth cone biomechanics and substrate rigidity response in peripheral and central nervous system neurons. Biophys. J. 102, 452-460 (2012).
    • (2012) Biophys. J. , vol.102 , pp. 452-460
    • Koch, D.1    Rosoff, W.J.2    Jiang, J.3    Geller, H.M.4    Urbach, J.S.5
  • 63
    • 67649336959 scopus 로고    scopus 로고
    • The structure of an interdomain complex that regulates talin activity
    • Goult, B. T. et al. The structure of an interdomain complex that regulates talin activity. J. Biol. Chem. 284, 15097-15106 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 15097-15106
    • Goult, B.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.