메뉴 건너뛰기




Volumn 7, Issue 4, 2012, Pages

Talin contains a C-terminal calpain2 cleavage site important in focal adhesion dynamics

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN 2; FOCAL ADHESION KINASE; GREEN FLUORESCENT PROTEIN; INTEGRIN; TALIN; ACTIN; CALPAIN; CAPN2 PROTEIN, HUMAN; TLN1 PROTEIN, HUMAN; TLN2 PROTEIN, HUMAN;

EID: 84859332670     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0034461     Document Type: Article
Times cited : (58)

References (58)
  • 1
    • 77952911072 scopus 로고    scopus 로고
    • Eukaryotic chemotaxis: a network of signaling pathways controls motility, directional sensing, and polarity
    • Swaney KF, Huang C-H, Devreotes PN, (2010) Eukaryotic chemotaxis: a network of signaling pathways controls motility, directional sensing, and polarity. Annual review of biophysics 39: 265-289.
    • (2010) Annual Review of Biophysics , vol.39 , pp. 265-289
    • Swaney, K.F.1    Huang, C.-H.2    Devreotes, P.N.3
  • 4
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: integrating cytoskeletal dynamics and cellular tension
    • Parsons JT, Horwitz AR, Schwartz MA, (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
  • 5
    • 1642586962 scopus 로고    scopus 로고
    • FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly
    • Webb DJ, Donais K, Whitmore LA, Thomas SM, Turner CE, et al. (2004) FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly. Nat Cell Biol 6: 154-161.
    • (2004) Nat Cell Biol , vol.6 , pp. 154-161
    • Webb, D.J.1    Donais, K.2    Whitmore, L.A.3    Thomas, S.M.4    Turner, C.E.5
  • 6
    • 65649146880 scopus 로고    scopus 로고
    • Integrin signalling at a glance
    • Harburger DS, Calderwood DA, (2009) Integrin signalling at a glance. J Cell Sci 122: 159-163.
    • (2009) J Cell Sci , vol.122 , pp. 159-163
    • Harburger, D.S.1    Calderwood, D.A.2
  • 8
    • 61449213806 scopus 로고    scopus 로고
    • Mechanisms that regulate adaptor binding to {beta}-integrin cytoplasmic tails
    • Legate KR, Fassler R, (2009) Mechanisms that regulate adaptor binding to {beta}-integrin cytoplasmic tails. J Cell Sci 122: 187-198.
    • (2009) J Cell Sci , vol.122 , pp. 187-198
    • Legate, K.R.1    Fassler, R.2
  • 10
    • 67650288199 scopus 로고    scopus 로고
    • Biochemical and structural properties of the integrin-associated cytoskeletal protein talin
    • Critchley DR, (2009) Biochemical and structural properties of the integrin-associated cytoskeletal protein talin. Annu Rev Biophys 38: 235-254.
    • (2009) Annu Rev Biophys , vol.38 , pp. 235-254
    • Critchley, D.R.1
  • 12
    • 77949862490 scopus 로고    scopus 로고
    • The final steps of integrin activation: the end game
    • Shattil SJ, Kim C, Ginsberg MH, (2010) The final steps of integrin activation: the end game. Nat Rev Mol Cell Biol 11: 288-300.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 288-300
    • Shattil, S.J.1    Kim, C.2    Ginsberg, M.H.3
  • 14
    • 61349122634 scopus 로고    scopus 로고
    • Talin 2 is a large and complex gene encoding multiple transcripts and protein isoforms
    • Debrand E, El Jai Y, Spence L, Bate N, Praekelt U, et al. (2009) Talin 2 is a large and complex gene encoding multiple transcripts and protein isoforms. FEBS J 276: 1610-1628.
    • (2009) FEBS J , vol.276 , pp. 1610-1628
    • Debrand, E.1    El Jai, Y.2    Spence, L.3    Bate, N.4    Praekelt, U.5
  • 15
    • 0032563558 scopus 로고    scopus 로고
    • Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated ES cells
    • Priddle H, Hemmings L, Monkley S, Woods A, Patel B, et al. (1998) Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated ES cells. J Cell Biol 142: 1121-1133.
    • (1998) J Cell Biol , vol.142 , pp. 1121-1133
    • Priddle, H.1    Hemmings, L.2    Monkley, S.3    Woods, A.4    Patel, B.5
  • 16
    • 77954957343 scopus 로고    scopus 로고
    • Studies on the morphology and spreading of human endothelial cells define key inter- and intramolecular interactions for talin1
    • Kopp PM, Bate N, Hansen TM, Brindle NP, Praekelt U, et al. (2010) Studies on the morphology and spreading of human endothelial cells define key inter- and intramolecular interactions for talin1. Eur J Cell Biol 89: 661-673.
    • (2010) Eur J Cell Biol , vol.89 , pp. 661-673
    • Kopp, P.M.1    Bate, N.2    Hansen, T.M.3    Brindle, N.P.4    Praekelt, U.5
  • 17
    • 51049100594 scopus 로고    scopus 로고
    • Talin depletion reveals independence of initial cell spreading from integrin activation and traction
    • Zhang X, Jiang G, Cai Y, Monkley SJ, Critchley DR, et al. (2008) Talin depletion reveals independence of initial cell spreading from integrin activation and traction. Nat Cell Biol 10: 1062-1068.
    • (2008) Nat Cell Biol , vol.10 , pp. 1062-1068
    • Zhang, X.1    Jiang, G.2    Cai, Y.3    Monkley, S.J.4    Critchley, D.R.5
  • 18
    • 0041461882 scopus 로고    scopus 로고
    • Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin
    • Jiang G, Giannone G, Critchley DR, Fukumoto E, Sheetz MP, (2003) Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 424: 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
  • 20
    • 70450222316 scopus 로고    scopus 로고
    • The structure of an integrin/talin complex reveals the basis of inside-out signal transduction
    • Anthis NJ, Wegener KL, Ye F, Kim C, Goult BT, et al. (2009) The structure of an integrin/talin complex reveals the basis of inside-out signal transduction. EMBO J 28: 3623-3632.
    • (2009) EMBO J , vol.28 , pp. 3623-3632
    • Anthis, N.J.1    Wegener, K.L.2    Ye, F.3    Kim, C.4    Goult, B.T.5
  • 21
    • 0033213922 scopus 로고    scopus 로고
    • The talin head domain binds to integrin b subunit cytoplasmic tails and regulates integrin activation
    • Calderwood DA, Zent R, Grant R, Rees DJG, Hynes RO, et al. (1999) The talin head domain binds to integrin b subunit cytoplasmic tails and regulates integrin activation. J Biol Chem 274: 28071-28704.
    • (1999) J Biol Chem , vol.274 , pp. 28071-28704
    • Calderwood, D.A.1    Zent, R.2    Grant, R.3    Rees, D.J.G.4    Hynes, R.O.5
  • 22
    • 4744343552 scopus 로고    scopus 로고
    • Characterization of an actin-binding site within the talin FERM domain
    • Lee HS, Bellin RM, Walker DL, Patel B, Powers P, et al. (2004) Characterization of an actin-binding site within the talin FERM domain. J Mol Biol 343: 771-784.
    • (2004) J Mol Biol , vol.343 , pp. 771-784
    • Lee, H.S.1    Bellin, R.M.2    Walker, D.L.3    Patel, B.4    Powers, P.5
  • 23
    • 0043234288 scopus 로고    scopus 로고
    • Phosphatidylinositol phosphate kinase type 1gamma and beta1-integrin cytoplasmic domain bind to the same region in the talin FERM domain
    • Barsukov IL, Prescot A, Bate N, Patel B, Floyd DN, et al. (2003) Phosphatidylinositol phosphate kinase type 1gamma and beta1-integrin cytoplasmic domain bind to the same region in the talin FERM domain. J Biol Chem 278: 31202-31209.
    • (2003) J Biol Chem , vol.278 , pp. 31202-31209
    • Barsukov, I.L.1    Prescot, A.2    Bate, N.3    Patel, B.4    Floyd, D.N.5
  • 24
    • 18644371169 scopus 로고    scopus 로고
    • Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin
    • Di Paolo G, Pellegrini L, Letinic K, Cestra G, Zoncu R, et al. (2002) Recruitment and regulation of phosphatidylinositol phosphate kinase type 1 gamma by the FERM domain of talin. Nature 420: 85-89.
    • (2002) Nature , vol.420 , pp. 85-89
    • Di Paolo, G.1    Pellegrini, L.2    Letinic, K.3    Cestra, G.4    Zoncu, R.5
  • 25
    • 0028146835 scopus 로고
    • Identification of functional domains in the cytoskeletal protein talin
    • Niggli V, Kaufmann S, Goldmann WH, Weber T, Isenberg G, (1994) Identification of functional domains in the cytoskeletal protein talin. Eur J Biochem 224: 3: 951-957.
    • (1994) Eur J Biochem , vol.224 , Issue.3 , pp. 951-957
    • Niggli, V.1    Kaufmann, S.2    Goldmann, W.H.3    Weber, T.4    Isenberg, G.5
  • 26
    • 77949566587 scopus 로고    scopus 로고
    • Structure of a double ubiquitin-like domain in the talin head: a role in integrin activation
    • Goult BT, Bouaouina M, Elliott PR, Bate N, Patel B, et al. (2010) Structure of a double ubiquitin-like domain in the talin head: a role in integrin activation. EMBO J 29: 1069-1080.
    • (2010) EMBO J , vol.29 , pp. 1069-1080
    • Goult, B.T.1    Bouaouina, M.2    Elliott, P.R.3    Bate, N.4    Patel, B.5
  • 27
  • 29
    • 4143083987 scopus 로고    scopus 로고
    • Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle
    • Papagrigoriou E, Gingras AR, Barsukov IL, Bate N, Fillingham IJ, et al. (2004) Activation of a vinculin-binding site in the talin rod involves rearrangement of a five-helix bundle. Embo J 23: 2942-2951.
    • (2004) Embo J , vol.23 , pp. 2942-2951
    • Papagrigoriou, E.1    Gingras, A.R.2    Barsukov, I.L.3    Bate, N.4    Fillingham, I.J.5
  • 30
    • 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, Rodius S, Coleman SJ, Monkley SJ, Goormaghtigh E, et al. (2007) 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) J Biol Chem , vol.282 , pp. 17280-17288
    • Moes, M.1    Rodius, S.2    Coleman, S.J.3    Monkley, S.J.4    Goormaghtigh, E.5
  • 32
    • 10544241952 scopus 로고    scopus 로고
    • Talin contains three actin-binding sites each of which is adjacent to a vinculin-binding site
    • Hemmings L, Rees DJG, Ohanian V, Bolton SJ, Gilmore AP, et al. (1996) Talin contains three actin-binding sites each of which is adjacent to a vinculin-binding site. J Cell Sci 109: 2715-2726.
    • (1996) J Cell Sci , vol.109 , pp. 2715-2726
    • Hemmings, L.1    Rees, D.J.G.2    Ohanian, V.3    Bolton, S.J.4    Gilmore, A.P.5
  • 33
    • 27744527513 scopus 로고    scopus 로고
    • Mapping and Consensus Sequence Identification for Multiple Vinculin Binding Sites within the Talin Rod
    • Gingras AR, Ziegler WH, Frank R, Barsukov IL, Roberts GC, et al. (2005) Mapping and Consensus Sequence Identification for Multiple Vinculin Binding Sites within the Talin Rod. J Biol Chem 280: 37217-37224.
    • (2005) J Biol Chem , vol.280 , pp. 37217-37224
    • Gingras, A.R.1    Ziegler, W.H.2    Frank, R.3    Barsukov, I.L.4    Roberts, G.C.5
  • 35
    • 0031929760 scopus 로고    scopus 로고
    • Vinculin knockout results in heart and brain defects during embryonic development
    • Xu W, Baribault H, Adamson ED, (1998) Vinculin knockout results in heart and brain defects during embryonic development. Development 125: 327-337.
    • (1998) Development , vol.125 , pp. 327-337
    • Xu, W.1    Baribault, H.2    Adamson, E.D.3
  • 36
    • 36849069902 scopus 로고    scopus 로고
    • Vinculin controls focal adhesion formation by direct interactions with talin and actin
    • Humphries JD, Wang P, Streuli C, Geiger B, Humphries MJ, et al. (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
  • 39
    • 0035930548 scopus 로고    scopus 로고
    • Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts
    • Dourdin N, Bhatt AK, Dutt P, Greer PA, Arthur JS, et al. (2001) Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J Biol Chem 276: 48382-48388.
    • (2001) J Biol Chem , vol.276 , pp. 48382-48388
    • Dourdin, N.1    Bhatt, A.K.2    Dutt, P.3    Greer, P.A.4    Arthur, J.S.5
  • 40
    • 33746155723 scopus 로고    scopus 로고
    • Calpain involvement in the remodeling of cytoskeletal anchorage complexes
    • Lebart M-C, Benyamin Y, (2006) Calpain involvement in the remodeling of cytoskeletal anchorage complexes. The FEBS journal 273: 3415-3426.
    • (2006) The FEBS Journal , vol.273 , pp. 3415-3426
    • Lebart, M.-C.1    Benyamin, Y.2
  • 42
    • 77951242361 scopus 로고    scopus 로고
    • Regulation of adhesion dynamics by calpain-mediated proteolysis of focal adhesion kinase (FAK)
    • Chan KT, Bennin DA, Huttenlocher A, (2010) Regulation of adhesion dynamics by calpain-mediated proteolysis of focal adhesion kinase (FAK). J Biol Chem 285: 11418-11426.
    • (2010) J Biol Chem , vol.285 , pp. 11418-11426
    • Chan, K.T.1    Bennin, D.A.2    Huttenlocher, A.3
  • 44
    • 78649788899 scopus 로고    scopus 로고
    • Calpain 2 controls turnover of LFA-1 adhesions on migrating T lymphocytes
    • Svensson L, McDowall A, Giles KM, Stanley P, Feske S, et al. (2010) Calpain 2 controls turnover of LFA-1 adhesions on migrating T lymphocytes. PloS one 5: e15090.
    • (2010) PloS One , vol.5
    • Svensson, L.1    McDowall, A.2    Giles, K.M.3    Stanley, P.4    Feske, S.5
  • 45
    • 33748948921 scopus 로고    scopus 로고
    • Calpain 2 and Src dependence distinguishes mesenchymal and amoeboid modes of tumour cell invasion: a link to integrin function
    • Carragher NO, Walker SM, Scott Carragher LA, Harris F, Sawyer TK, et al. (2006) Calpain 2 and Src dependence distinguishes mesenchymal and amoeboid modes of tumour cell invasion: a link to integrin function. Oncogene 25: 5726-5740.
    • (2006) Oncogene , vol.25 , pp. 5726-5740
    • Carragher, N.O.1    Walker, S.M.2    Scott, C.L.A.3    Harris, F.4    Sawyer, T.K.5
  • 47
    • 65449148205 scopus 로고    scopus 로고
    • Talin phosphorylation by Cdk5 regulates Smurf1-mediated talin head ubiquitylation and cell migration
    • Huang C, Rajfur Z, Yousefi N, Chen Z, Jacobson K, et al. (2009) Talin phosphorylation by Cdk5 regulates Smurf1-mediated talin head ubiquitylation and cell migration. Nat Cell Biol 11: 624-630.
    • (2009) Nat Cell Biol , vol.11 , pp. 624-630
    • Huang, C.1    Rajfur, Z.2    Yousefi, N.3    Chen, Z.4    Jacobson, K.5
  • 48
    • 0033571776 scopus 로고    scopus 로고
    • The behavior of calpain-generated N- and C-terminal fragments of talin in integrin-mediated signaling pathways
    • Hayashi M, Suzuki H, Kawashima S, Saido TC, Inomata M, (1999) The behavior of calpain-generated N- and C-terminal fragments of talin in integrin-mediated signaling pathways. Arch Biochem Biophys 371: 133-141.
    • (1999) Arch Biochem Biophys , vol.371 , pp. 133-141
    • Hayashi, M.1    Suzuki, H.2    Kawashima, S.3    Saido, T.C.4    Inomata, M.5
  • 49
    • 1842378589 scopus 로고    scopus 로고
    • Monoclonal Antibodies Recognizing the N- and C- Terminal Regions of Talin Disrupt Actin Stress Fibers when Microinjected into Human Fibroblasts
    • Bolton SJ, Barry ST, Mosley H, Patel B, Jockusch B, et al. (1997) Monoclonal Antibodies Recognizing the N- and C- Terminal Regions of Talin Disrupt Actin Stress Fibers when Microinjected into Human Fibroblasts. Cell Motil Cytoskeleton 36: 363-376.
    • (1997) Cell Motil Cytoskeleton , vol.36 , pp. 363-376
    • Bolton, S.J.1    Barry, S.T.2    Mosley, H.3    Patel, B.4    Jockusch, B.5
  • 51
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A, Blundell TL, (1993) Comparative protein modelling by satisfaction of spatial restraints. Journal of molecular biology 234: 779-815.
    • (1993) Journal of Molecular Biology , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 52
    • 33847217997 scopus 로고    scopus 로고
    • Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle
    • Senetar MA, Moncman CL, McCann RO, (2007) Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle. Cell Motil Cytoskeleton 64: 157-173.
    • (2007) Cell Motil Cytoskeleton , vol.64 , pp. 157-173
    • Senetar, M.A.1    Moncman, C.L.2    McCann, R.O.3
  • 53
    • 0031031730 scopus 로고    scopus 로고
    • Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility
    • Stabach PR, Cianci CD, Glantz SB, Zhang Z, Morrow JS, (1997) Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility. Biochemistry 36: 57-65.
    • (1997) Biochemistry , vol.36 , pp. 57-65
    • Stabach, P.R.1    Cianci, C.D.2    Glantz, S.B.3    Zhang, Z.4    Morrow, J.S.5
  • 54
    • 84855737428 scopus 로고    scopus 로고
    • The C-terminus of talin links integrins to cell cycle progression
    • Wang P, Ballestrem C, Streuli CH, (2011) The C-terminus of talin links integrins to cell cycle progression. J Cell Biol 195: 499-513.
    • (2011) J Cell Biol , vol.195 , pp. 499-513
    • Wang, P.1    Ballestrem, C.2    Streuli, C.H.3
  • 55
    • 77958502543 scopus 로고    scopus 로고
    • m-Calpain activation is regulated by its membrane localization and by its binding to phosphatidylinositol 4,5-bisphosphate
    • Leloup L, Shao H, Bae YH, Deasy B, Stolz D, et al. (2010) m-Calpain activation is regulated by its membrane localization and by its binding to phosphatidylinositol 4,5-bisphosphate. The Journal of biological chemistry 285: 33549-33566.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 33549-33566
    • Leloup, L.1    Shao, H.2    Bae, Y.H.3    Deasy, B.4    Stolz, D.5
  • 58
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: development of a software pipeline
    • Vranken WF, Boucher W, Stevens TJ, Fogh RH, Pajon A, et al. (2005) The CCPN data model for NMR spectroscopy: development of a software pipeline. Proteins 59: 687-696.
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1    Boucher, W.2    Stevens, T.J.3    Fogh, R.H.4    Pajon, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.