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Volumn 63, Issue 9, 2006, Pages 563-581

The conserved C-terminal I/LWEQ module targets Talin1 to focal adhesions

Author keywords

Actin; Actin binding protein; Cytoskeleton; Integrin; Talin

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; TALIN; TALIN 1; UNCLASSIFIED DRUG;

EID: 33748713060     PISSN: 08861544     EISSN: 10970169     Source Type: Journal    
DOI: 10.1002/cm.20145     Document Type: Article
Times cited : (21)

References (74)
  • 1
    • 0029086272 scopus 로고
    • Down regulation of talin alters cell adhesion and the processing of the α5 β1 integrin
    • Albiges-Rizo C, Frachet P, Block MR. 1995. Down regulation of talin alters cell adhesion and the processing of the α5 β1 integrin. J Cell Sci 108:3317-3329.
    • (1995) J Cell Sci , vol.108 , pp. 3317-3329
    • Albiges-Rizo, C.1    Frachet, P.2    Block, M.R.3
  • 2
    • 0033565992 scopus 로고    scopus 로고
    • Talin contains three similar vinculin-binding sites predicted to form an amphipathic helix
    • Bass MD, Smith BJ, Prigent SA, Critchley DR. 1999. Talin contains three similar vinculin-binding sites predicted to form an amphipathic helix. Biochem J 341:257-263.
    • (1999) Biochem J , vol.341 , pp. 257-263
    • Bass, M.D.1    Smith, B.J.2    Prigent, S.A.3    Critchley, D.R.4
  • 3
    • 0032547737 scopus 로고    scopus 로고
    • Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles
    • Borowsky ML, Hynes RO. 1998. Layilin, a novel talin-binding transmembrane protein homologous with C-type lectins, is localized in membrane ruffles. J Cell Biol 143:429-442.
    • (1998) J Cell Biol , vol.143 , pp. 429-442
    • Borowsky, M.L.1    Hynes, R.O.2
  • 4
    • 0031471375 scopus 로고    scopus 로고
    • Ezrin: A protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures
    • Bretscher A, Reczek D, Berryman M. 1997. Ezrin: A protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J Cell Sci 110:3011-3018.
    • (1997) J Cell Sci , vol.110 , pp. 3011-3018
    • Bretscher, A.1    Reczek, D.2    Berryman, M.3
  • 6
    • 0020805412 scopus 로고
    • A new protein of adhesion plaques and ruffling membranes
    • Burridge K, Connell L. 1983. A new protein of adhesion plaques and ruffling membranes. J Cell Biol 97:359-367.
    • (1983) J Cell Biol , vol.97 , pp. 359-367
    • Burridge, K.1    Connell, L.2
  • 7
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • Calderwood DA. 2004. Integrin activation. J Cell Sci 117:657-666.
    • (2004) J Cell Sci , vol.117 , pp. 657-666
    • Calderwood, D.A.1
  • 8
    • 0033213922 scopus 로고    scopus 로고
    • The talin head domain binds to integrin β subunit cytoplasmic tails and regulates integrin activation
    • Calderwood DA, Zent R, Grant R, Rees DJ, Hynes RO, Ginsberg MH. 1999. The talin head domain binds to integrin β subunit cytoplasmic tails and regulates integrin activation. J Biol Chem 274:28071-28074.
    • (1999) J Biol Chem , vol.274 , pp. 28071-28074
    • Calderwood, D.A.1    Zent, R.2    Grant, R.3    Rees, D.J.4    Hynes, R.O.5    Ginsberg, M.H.6
  • 10
    • 0033229742 scopus 로고    scopus 로고
    • Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp125(FAK), paxillin, and talin
    • Carragher NO, Levkau B, Ross R, Raines EW. 1999. Degraded collagen fragments promote rapid disassembly of smooth muscle focal adhesions that correlates with cleavage of pp125(FAK), paxillin, and talin. J Cell Biol 147:619-630.
    • (1999) J Cell Biol , vol.147 , pp. 619-630
    • Carragher, N.O.1    Levkau, B.2    Ross, R.3    Raines, E.W.4
  • 11
    • 0035688044 scopus 로고    scopus 로고
    • Role of αVβ3 integrin receptor in the invasive potential of human cervical (SiHa) cells
    • Chatterjee N, Chatterjee A. 2001. Role of αVβ3 integrin receptor in the invasive potential of human cervical (SiHa) cells. J Environ Pathol Toxicol Oncol 20:211-221.
    • (2001) J Environ Pathol Toxicol Oncol , vol.20 , pp. 211-221
    • Chatterjee, N.1    Chatterjee, A.2
  • 15
    • 20444492339 scopus 로고    scopus 로고
    • Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin
    • Cohen DM, Chen H, Johnson RP, Choudhury B, Craig SW. 2005. Two distinct head-tail interfaces cooperate to suppress activation of vinculin by talin. J Biol Chem 280:17109-17117.
    • (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
  • 16
    • 0037350396 scopus 로고    scopus 로고
    • TES is a novel focal adhesion protein with a role in cell spreading
    • Coutts A, MacKenzie E, Griffith E, Black D. 2003. TES is a novel focal adhesion protein with a role in cell spreading. J Cell Sci 116:897-906.
    • (2003) J Cell Sci , vol.116 , pp. 897-906
    • Coutts, A.1    MacKenzie, E.2    Griffith, E.3    Black, D.4
  • 17
    • 0030067021 scopus 로고    scopus 로고
    • Assembly of focal adhesions: Progress, paradigms, and portents
    • Craig SW, Johnson RP. 1996. Assembly of focal adhesions: Progress, paradigms, and portents. Curr Opin Cell Biol 8:74-85.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 74-85
    • Craig, S.W.1    Johnson, R.P.2
  • 18
    • 0142106350 scopus 로고    scopus 로고
    • Talin loss-of-function uncovers roles in cell contractility and migration in C. elegans
    • Cram EJ, Clark SG, Schwarzbauer JE. 2003. Talin loss-of-function uncovers roles in cell contractility and migration in C. elegans. J Cell Sci 116:3871-3878.
    • (2003) J Cell Sci , vol.116 , pp. 3871-3878
    • Cram, E.J.1    Clark, S.G.2    Schwarzbauer, J.E.3
  • 19
    • 0033962672 scopus 로고    scopus 로고
    • Focal adhesions - The cytoskeletal connection
    • Critchley DR. 2000. Focal adhesions-The cytoskeletal connection. Curr Opin Cell Biol 12:133-139.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 133-139
    • Critchley, D.R.1
  • 20
    • 8744300054 scopus 로고    scopus 로고
    • Cytoskeletal proteins talin and vinculin in integrin-mediated adhesion
    • Critchley DR. 2004. Cytoskeletal proteins talin and vinculin in integrin-mediated adhesion. Biochem Soc Trans 32:831-836.
    • (2004) Biochem Soc Trans , vol.32 , pp. 831-836
    • Critchley, D.R.1
  • 22
    • 0033611051 scopus 로고    scopus 로고
    • An actin-binding protein of the Sla2/huntingtin interacting protein-1 family is a novel component of clathrin-coated pits and vesicles
    • Engqvist-Goldstein AE, Kessels MM, Chopra VS, Hayden MR, Drubin DG. 1999. An actin-binding protein of the Sla2/huntingtin interacting protein-1 family is a novel component of clathrin-coated pits and vesicles. J Cell Biol 147:1503-1518.
    • (1999) J Cell Biol , vol.147 , pp. 1503-1518
    • Engqvist-Goldstein, A.E.1    Kessels, M.M.2    Chopra, V.S.3    Hayden, M.R.4    Drubin, D.G.5
  • 23
    • 4043077024 scopus 로고    scopus 로고
    • Isoform specific function of calpain 2 in regulating membrane protrusion
    • Franco SJ, Perrin BJ, Huttenlocher A. 2004a. Isoform specific function of calpain 2 in regulating membrane protrusion. Exp Cell Res 299:179-187.
    • (2004) Exp Cell Res , vol.299 , pp. 179-187
    • Franco, S.J.1    Perrin, B.J.2    Huttenlocher, A.3
  • 25
    • 0033794569 scopus 로고    scopus 로고
    • Complexity and specificity of integrin signalling
    • Giancotti FG. 2000. Complexity and specificity of integrin signalling. Nat Cell Biol 2:E13-E14.
    • (2000) Nat Cell Biol , vol.2
    • Giancotti, F.G.1
  • 27
    • 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, Roberts GCK, Critchley DR, Emsley J. 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    Roberts, G.C.K.4    Critchley, D.R.5    Emsley, J.6
  • 28
    • 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
  • 30
    • 0028825276 scopus 로고
    • Automated construction and graphical presentation of protein blocks from unaligned sequences
    • Henikoff S, Henikoff JG, Alford WJ, Pietrokovski S. 1995. Automated construction and graphical presentation of protein blocks from unaligned sequences. Gene 163:GC17-GC26.
    • (1995) Gene , vol.163
    • Henikoff, S.1    Henikoff, J.G.2    Alford, W.J.3    Pietrokovski, S.4
  • 31
    • 0034715891 scopus 로고    scopus 로고
    • Multiple roles of integrins in cell motility
    • Holly SP, Larson MK, LV P. 2000. Multiple roles of integrins in cell motility. Exp Cell Res 261:69-74.
    • (2000) Exp Cell Res , vol.261 , pp. 69-74
    • Holly, S.P.1    Larson, M.K.2    P, L.V.3
  • 32
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin-A transmembrane linkage
    • Horwitz A, Duggan K, Buck C, Beckerle MC, Burridge K. 1986. Interaction of plasma membrane fibronectin receptor with talin-A transmembrane linkage. Nature 320:531-533.
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 33
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes RO. 1992. Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 34
    • 3042600016 scopus 로고    scopus 로고
    • Structural basis for amplifying vinculin activation by talin
    • Izard T, Vonrhein C. 2004. Structural basis for amplifying vinculin activation by talin. J Biol Chem 27667-27678.
    • (2004) J Biol Chem , pp. 27667-27678
    • Izard, T.1    Vonrhein, C.2
  • 36
    • 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
  • 37
    • 0032531432 scopus 로고    scopus 로고
    • Human integrin αVβ3 gene expression: Evidence for a megakaryocytic cell-specific cis-acting element
    • Jin Y, Wilhide C, Dang C, Li L, Li S, Villa-Garcia M, Bray PF. 1998. Human integrin αVβ3 gene expression: Evidence for a megakaryocytic cell-specific cis-acting element. Blood 92:2777-2790.
    • (1998) Blood , vol.92 , pp. 2777-2790
    • Jin, Y.1    Wilhide, C.2    Dang, C.3    Li, L.4    Li, S.5    Villa-Garcia, M.6    Bray, P.F.7
  • 38
    • 0028318397 scopus 로고
    • An intramolecular association between the head and tail domains of vinculin modulates talin binding
    • Johnson RP, Craig SW. 1994. An intramolecular association between the head and tail domains of vinculin modulates talin binding. J Biol Chem 269:12611-12619.
    • (1994) J Biol Chem , vol.269 , pp. 12611-12619
    • Johnson, R.P.1    Craig, S.W.2
  • 39
    • 0029009673 scopus 로고
    • The carboxy-terminal tail domain of vinculin contains a cryptic binding site for acidic phospholipids
    • Johnson RP, Craig SW. 1995. The carboxy-terminal tail domain of vinculin contains a cryptic binding site for acidic phospholipids. Biochem Biophys Res Commun 210:159-164.
    • (1995) Biochem Biophys Res Commun , vol.210 , pp. 159-164
    • Johnson, R.P.1    Craig, S.W.2
  • 42
    • 0037038412 scopus 로고    scopus 로고
    • Type I γ phosphatidylinositol phosphate kinase targets and regulates focal adhesions
    • Ling K, Doughman RL, Firestone AJ, Bunce MW, Anderson RA. 2002. Type I γ phosphatidylinositol phosphate kinase targets and regulates focal adhesions. Nature 420:89-93.
    • (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
  • 43
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-binding proteins
    • Liu S, Calderwood DA, Ginsberg MH. 2000. Integrin cytoplasmic domain-binding proteins. J Cell Sci 113:3563-3571.
    • (2000) J Cell Sci , vol.113 , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2    Ginsberg, M.H.3
  • 44
    • 0019135186 scopus 로고
    • Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association
    • MacLean-Fletcher S, Pollard TD. 1980. Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association. Biochem Biophys Res Commun 96:18-27.
    • (1980) Biochem Biophys Res Commun , vol.96 , pp. 18-27
    • MacLean-Fletcher, S.1    Pollard, T.D.2
  • 46
    • 0030908297 scopus 로고    scopus 로고
    • The I/LWEQ module: A conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals
    • McCann RO, Craig SW. 1997. The I/LWEQ module: A conserved sequence that signifies F-actin binding in functionally diverse proteins from yeast to mammals. Proc Natl Acad Sci USA 94:5679-5684.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 5679-5684
    • McCann, R.O.1    Craig, S.W.2
  • 47
    • 0033539916 scopus 로고    scopus 로고
    • Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein: Actin interaction
    • McCann RO, Craig SW. 1999. Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein: Actin interaction. Biochem Biophys Res Commun 266:135-140.
    • (1999) Biochem Biophys Res Commun , vol.266 , pp. 135-140
    • McCann, R.O.1    Craig, S.W.2
  • 49
    • 0036222549 scopus 로고    scopus 로고
    • Sensing the environment: A historical perspective on integrin signal transduction
    • Miranti CK, Brugge JS. 2002. Sensing the environment: A historical perspective on integrin signal transduction. Nat Cell Biol 4:83-90.
    • (2002) Nat Cell Biol , vol.4 , pp. 83-90
    • Miranti, C.K.1    Brugge, J.S.2
  • 53
    • 0025313592 scopus 로고
    • Functional studies of the domains of talin
    • Nuckolls GH, Turner CE, Burridge K. 1990. Functional studies of the domains of talin. J Cell Biol 110:1635-1644.
    • (1990) J Cell Biol , vol.110 , pp. 1635-1644
    • Nuckolls, G.H.1    Turner, C.E.2    Burridge, K.3
  • 54
    • 0026641590 scopus 로고
    • Microinjection of antibodies against talin inhibits the spreading and migration of fibroblasts
    • Nuckolls GH, Romer LH, Burridge K. 1992. Microinjection of antibodies against talin inhibits the spreading and migration of fibroblasts. J Cell Sci 102:753-762.
    • (1992) J Cell Sci , vol.102 , pp. 753-762
    • Nuckolls, G.H.1    Romer, L.H.2    Burridge, K.3
  • 55
    • 0021931061 scopus 로고
    • Identification of talin as a major cytoplasmic protein implicated in platelet activation
    • O'Halloran T, Beckerle MC, Burridge K. 1985. Identification of talin as a major cytoplasmic protein implicated in platelet activation. Nature 317:449-451.
    • (1985) Nature , vol.317 , pp. 449-451
    • O'Halloran, T.1    Beckerle, M.C.2    Burridge, K.3
  • 56
    • 0034693854 scopus 로고    scopus 로고
    • Focal adhesion kinase: A regulator of focal adhesion dynamics and cell movement
    • Parsons JT, Martin KH, Slack JK, Taylor JM, Weed SA. 2000. Focal adhesion kinase: A regulator of focal adhesion dynamics and cell movement. Oncogene 19:5606-5613.
    • (2000) Oncogene , vol.19 , pp. 5606-5613
    • Parsons, J.T.1    Martin, K.H.2    Slack, J.K.3    Taylor, J.M.4    Weed, S.A.5
  • 58
    • 0034724536 scopus 로고    scopus 로고
    • Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain
    • Pearson MA, Reczek D, Bretscher A, Karplus PA. 2000. Structure of the ERM protein moesin reveals the FERM domain fold masked by an extended actin binding tail domain. Cell 101:259-270.
    • (2000) Cell , vol.101 , pp. 259-270
    • Pearson, M.A.1    Reczek, D.2    Bretscher, A.3    Karplus, P.A.4
  • 59
    • 0032563558 scopus 로고    scopus 로고
    • Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated embryonic stem cells
    • Priddle H, Hemmings L, Monkley S, Woods A, Patel B, Sutton D, Dunn GA, Zicha D, Critchley DR. 1998. Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated embryonic stem 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    Sutton, D.6    Dunn, G.A.7    Zicha, D.8    Critchley, D.R.9
  • 62
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B, Sander C. 1994. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19:55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 63
    • 0034715923 scopus 로고    scopus 로고
    • Focal adhesions: A nexus for intracellular signaling and cytoskeletal dynamics
    • Sastry SK, Burridge K. 2000. Focal adhesions: A nexus for intracellular signaling and cytoskeletal dynamics. Exp Cell Res 261:25-36.
    • (2000) Exp Cell Res , vol.261 , pp. 25-36
    • Sastry, S.K.1    Burridge, K.2
  • 65
    • 28244491001 scopus 로고    scopus 로고
    • Gene duplication and functional divergence during evolution of the cytoskeletal linker protein talin
    • Senetar MA, McCann RO. 2005. Gene duplication and functional divergence during evolution of the cytoskeletal linker protein talin. Gene 362:141-152.
    • (2005) Gene , vol.362 , pp. 141-152
    • Senetar, M.A.1    McCann, R.O.2
  • 66
    • 10644221869 scopus 로고    scopus 로고
    • Intrasteric inhibition mediates the interaction of the I/LWEQ module proteins Talin 1, Talin2, Hip1, and Hip12 with actin
    • Senetar MA, Foster SJ, McCann RO. 2004. Intrasteric inhibition mediates the interaction of the I/LWEQ module proteins Talin 1, Talin2, Hip1, and Hip12 with actin. Biochemistry 43:15418-15428.
    • (2004) Biochemistry , vol.43 , pp. 15418-15428
    • Senetar, M.A.1    Foster, S.J.2    McCann, R.O.3
  • 67
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich JA, Watt S. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 246:4866-4871.
    • (1971) J Biol Chem , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 69
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 70
    • 2542419770 scopus 로고    scopus 로고
    • A fluorescence cell biology approach to map the second integrin-binding site of talin to a 130 amino acid sequence with the rod domain
    • Tremuth L, Kreis S, Melchior C, Hoebeke J, Ronde P, Plancon S, Takeda K, Kieffer N. 2004. A fluorescence cell biology approach to map the second integrin-binding site of talin to a 130 amino acid sequence with the rod domain. J Biol Chem 279:22258-22266.
    • (2004) J Biol Chem , vol.279 , pp. 22258-22266
    • Tremuth, L.1    Kreis, S.2    Melchior, C.3    Hoebeke, J.4    Ronde, P.5    Plancon, S.6    Takeda, K.7    Kieffer, N.8
  • 71
    • 0031033956 scopus 로고    scopus 로고
    • Energy-filtered electron microscopy reveals that talin is a highly flexible protein composed of a series of globular domains
    • Winkler J, Lunsdorf H, Jockusch BM. 1997. Energy-filtered electron microscopy reveals that talin is a highly flexible protein composed of a series of globular domains. Eur J Biochem 243:430-436.
    • (1997) Eur J Biochem , vol.243 , pp. 430-436
    • Winkler, J.1    Lunsdorf, H.2    Jockusch, B.M.3
  • 72
    • 0035976972 scopus 로고    scopus 로고
    • Localization of an integrin binding site to the C terminus of talin
    • Xing B, Jedsadayanmata A, Lam SC. 2001. Localization of an integrin binding site to the C terminus of talin. J Biol Chem 276:44373-44378.
    • (2001) J Biol Chem , vol.276 , pp. 44373-44378
    • Xing, B.1    Jedsadayanmata, A.2    Lam, S.C.3
  • 73
    • 0035958967 scopus 로고    scopus 로고
    • Calpain cleavage promotes talin binding to the β3 integrin cytoplasmic domain
    • Yan B, Calderwood DA, Yaspan B, Ginsberg MH. 2001. Calpain cleavage promotes talin binding to the β3 integrin cytoplasmic domain. J Biol Chem 276:28164-28170.
    • (2001) J Biol Chem , vol.276 , pp. 28164-28170
    • Yan, B.1    Calderwood, D.A.2    Yaspan, B.3    Ginsberg, M.H.4
  • 74
    • 0032589216 scopus 로고    scopus 로고
    • Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals
    • Yang S, Cope MI, Drubin DG. 1999. Sla2p is associated with the yeast cortical actin cytoskeleton via redundant localization signals. Mol Biol Cell 10:2265-2283.
    • (1999) Mol Biol Cell , vol.10 , pp. 2265-2283
    • Yang, S.1    Cope, M.I.2    Drubin, D.G.3


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