메뉴 건너뛰기




Volumn 7, Issue 3, 2012, Pages

Kindlins, integrin activation and the regulation of talin recruitment to αIIbβ3

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA2B BETA3 INTEGRIN; GLYCOPROTEIN; KINDLIN; KINDLIN 2; KINDLIN 3; MEMBRANE PROTEIN; PROTEINASE ACTIVATED RECEPTOR 1; SHORT HAIRPIN RNA; TALIN; UNCLASSIFIED DRUG; BETA3 INTEGRIN; FERMT1 PROTEIN, HUMAN; GLYCOPROTEIN IIB; TUMOR PROTEIN;

EID: 84858779307     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0034056     Document Type: Article
Times cited : (52)

References (54)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes RO, (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110: 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 2
    • 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
  • 3
    • 0027757072 scopus 로고
    • Talin distribution and phosphorylation in thrombin-activated platelets
    • Bertagnolli ME, Locke SJ, Hensler ME, Bray PF, Beckerle MC, (1993) Talin distribution and phosphorylation in thrombin-activated platelets. J Cell Sci 106 (Pt 4): 1189-1199.
    • (1993) J Cell Sci , vol.106 , Issue.Pt 4 , pp. 1189-1199
    • Bertagnolli, M.E.1    Locke, S.J.2    Hensler, M.E.3    Bray, P.F.4    Beckerle, M.C.5
  • 4
    • 67649336959 scopus 로고    scopus 로고
    • The structure of an interdomain complex that regulates talin activity
    • Goult BT, Bate N, Anthis NJ, Wegener KL, Gingras AR, et al. (2009) The structure of an interdomain complex that regulates talin activity. J Biol Chem 284: 15097-15106.
    • (2009) J Biol Chem , vol.284 , pp. 15097-15106
    • Goult, B.T.1    Bate, N.2    Anthis, N.J.3    Wegener, K.L.4    Gingras, A.R.5
  • 5
    • 46149093439 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of talin in regulating integrin activation
    • Goksoy E, Ma YQ, Wang X, Kong X, Perera D, et al. (2008) Structural basis for the autoinhibition of talin in regulating integrin activation. Mol Cell 31: 124-133.
    • (2008) Mol Cell , vol.31 , pp. 124-133
    • Goksoy, E.1    Ma, Y.Q.2    Wang, X.3    Kong, X.4    Perera, D.5
  • 6
    • 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
  • 7
    • 72949089800 scopus 로고    scopus 로고
    • Structural and biophysical properties of the integrin-associated cytoskeletal protein talin
    • Roberts GC, Critchley DR, (2009) Structural and biophysical properties of the integrin-associated cytoskeletal protein talin. Biophys Rev 1: 61-69.
    • (2009) Biophys Rev , vol.1 , pp. 61-69
    • Roberts, G.C.1    Critchley, D.R.2
  • 8
    • 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
  • 10
    • 52649163308 scopus 로고    scopus 로고
    • CalDAG-GEFI and protein kinase C represent alternative pathways leading to activation of integrin alphaIIbbeta3 in platelets
    • Cifuni SM, Wagner DD, Bergmeier W, (2008) CalDAG-GEFI and protein kinase C represent alternative pathways leading to activation of integrin alphaIIbbeta3 in platelets. Blood 112: 1696-1703.
    • (2008) Blood , vol.112 , pp. 1696-1703
    • Cifuni, S.M.1    Wagner, D.D.2    Bergmeier, W.3
  • 11
    • 46249121793 scopus 로고    scopus 로고
    • Mechanisms and consequences of agonist-induced talin recruitment to platelet integrin alphaIIbbeta3
    • Watanabe N, Bodin L, Pandey M, Krause M, Coughlin S, et al. (2008) Mechanisms and consequences of agonist-induced talin recruitment to platelet integrin alphaIIbbeta3. J Cell Biol 181: 1211-1222.
    • (2008) J Cell Biol , vol.181 , pp. 1211-1222
    • Watanabe, N.1    Bodin, L.2    Pandey, M.3    Krause, M.4    Coughlin, S.5
  • 12
    • 33748454742 scopus 로고    scopus 로고
    • Reconstructing and deconstructing agonist-induced activation of integrin alphaIIbbeta3
    • Han J, Lim CJ, Watanabe N, Soriani A, Ratnikov B, et al. (2006) Reconstructing and deconstructing agonist-induced activation of integrin alphaIIbbeta3. Curr Biol 16: 1796-1806.
    • (2006) Curr Biol , vol.16 , pp. 1796-1806
    • Han, J.1    Lim, C.J.2    Watanabe, N.3    Soriani, A.4    Ratnikov, B.5
  • 13
    • 64149100431 scopus 로고    scopus 로고
    • RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences
    • Lee HS, Lim CJ, Puzon-McLaughlin W, Shattil SJ, Ginsberg MH, (2009) RIAM activates integrins by linking talin to ras GTPase membrane-targeting sequences. J Biol Chem 284: 5119-5127.
    • (2009) J Biol Chem , vol.284 , pp. 5119-5127
    • Lee, H.S.1    Lim, C.J.2    Puzon-McLaughlin, W.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 14
    • 77957777260 scopus 로고    scopus 로고
    • The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study
    • Kalli AC, Wegener KL, Goult BT, Anthis NJ, Campbell ID, et al. (2010) The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study. Structure 18: 1280-1288.
    • (2010) Structure , vol.18 , pp. 1280-1288
    • Kalli, A.C.1    Wegener, K.L.2    Goult, B.T.3    Anthis, N.J.4    Campbell, I.D.5
  • 15
    • 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
  • 16
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • Lau TL, Kim C, Ginsberg MH, Ulmer TS, (2009) The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling. Embo J 28: 1351-1361.
    • (2009) Embo J , vol.28 , pp. 1351-1361
    • Lau, T.L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 17
    • 75749154495 scopus 로고    scopus 로고
    • Recreation of the terminal events in physiological integrin activation
    • Ye F, Hu G, Taylor D, Ratnikov B, Bobkov AA, et al. (2010) Recreation of the terminal events in physiological integrin activation. J Cell Biol 188: 157-173.
    • (2010) J Cell Biol , vol.188 , pp. 157-173
    • Ye, F.1    Hu, G.2    Taylor, D.3    Ratnikov, B.4    Bobkov, A.A.5
  • 18
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • Moser M, Nieswandt B, Ussar S, Pozgajova M, Fassler R, (2008) Kindlin-3 is essential for integrin activation and platelet aggregation. Nat Med 14: 325-330.
    • (2008) Nat Med , vol.14 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fassler, R.5
  • 19
    • 61949352480 scopus 로고    scopus 로고
    • Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells
    • Moser M, Bauer M, Schmid S, Ruppert R, Schmidt S, et al. (2009) Kindlin-3 is required for beta2 integrin-mediated leukocyte adhesion to endothelial cells. Nat Med 15: 300-305.
    • (2009) Nat Med , vol.15 , pp. 300-305
    • Moser, M.1    Bauer, M.2    Schmid, S.3    Ruppert, R.4    Schmidt, S.5
  • 20
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser M, Legate KR, Zent R, Fassler R, (2009) The tail of integrins, talin, and kindlins. Science 324: 895-899.
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4
  • 21
    • 43149085289 scopus 로고    scopus 로고
    • Kindlin-2 (Mig-2): a co-activator of beta3 integrins
    • Ma YQ, Qin J, Wu C, Plow EF, (2008) Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J Cell Biol 181: 439-446.
    • (2008) J Cell Biol , vol.181 , pp. 439-446
    • Ma, Y.Q.1    Qin, J.2    Wu, C.3    Plow, E.F.4
  • 22
    • 66449119343 scopus 로고    scopus 로고
    • Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects
    • Harburger DS, Bouaouina M, Calderwood DA, (2009) Kindlin-1 and-2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects. J Biol Chem 284: 11485-11497.
    • (2009) J Biol Chem , vol.284 , pp. 11485-11497
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 23
    • 34547120497 scopus 로고    scopus 로고
    • The MIG-2/integrin interaction strengthens cell-matrix adhesion and modulates cell motility
    • Shi X, Ma YQ, Tu Y, Chen K, Wu S, et al. (2007) The MIG-2/integrin interaction strengthens cell-matrix adhesion and modulates cell motility. J Biol Chem 282: 20455-20466.
    • (2007) J Biol Chem , vol.282 , pp. 20455-20466
    • Shi, X.1    Ma, Y.Q.2    Tu, Y.3    Chen, K.4    Wu, S.5
  • 24
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • Tu Y, Wu S, Shi X, Chen K, Wu C, (2003) Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell 113: 37-47.
    • (2003) Cell , vol.113 , pp. 37-47
    • Tu, Y.1    Wu, S.2    Shi, X.3    Chen, K.4    Wu, C.5
  • 25
    • 80051802621 scopus 로고    scopus 로고
    • Kindlin: helper, co-activator, or booster of talin in integrin activation?
    • Ye F, Petrich BG, (2011) Kindlin: helper, co-activator, or booster of talin in integrin activation? Curr Opin Hematol 18: 356-360.
    • (2011) Curr Opin Hematol , vol.18 , pp. 356-360
    • Ye, F.1    Petrich, B.G.2
  • 26
    • 0026035523 scopus 로고
    • Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation
    • Vu TK, Hung DT, Wheaton VI, Coughlin SR, (1991) Molecular cloning of a functional thrombin receptor reveals a novel proteolytic mechanism of receptor activation. Cell 64: 1057-1068.
    • (1991) Cell , vol.64 , pp. 1057-1068
    • Vu, T.K.1    Hung, D.T.2    Wheaton, V.I.3    Coughlin, S.R.4
  • 27
    • 0029966310 scopus 로고    scopus 로고
    • Breaking the integrin hinge. A defined structural constraint regulates integrin signaling
    • Hughes PE, Diaz-Gonzalez F, Leong L, Wu C, McDonald JA, et al. (1996) Breaking the integrin hinge. A defined structural constraint regulates integrin signaling. J Biol Chem 271: 6571-6574.
    • (1996) J Biol Chem , vol.271 , pp. 6571-6574
    • Hughes, P.E.1    Diaz-Gonzalez, F.2    Leong, L.3    Wu, C.4    McDonald, J.A.5
  • 28
    • 0028285015 scopus 로고
    • Integrin cytoplasmic domains mediate inside-out signal transduction
    • O'Toole TE, Katagiri Y, Faull RJ, Peter K, Tamura R, et al. (1994) Integrin cytoplasmic domains mediate inside-out signal transduction. J Cell Biol 124: 1047-1059.
    • (1994) J Cell Biol , vol.124 , pp. 1047-1059
    • O'Toole, T.E.1    Katagiri, Y.2    Faull, R.J.3    Peter, K.4    Tamura, R.5
  • 29
    • 0022180156 scopus 로고
    • Changes in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation
    • Shattil SJ, Hoxie JA, Cunningham M, Brass LF, (1985) Changes in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation. J Biol Chem 260: 11107-11114.
    • (1985) J Biol Chem , vol.260 , pp. 11107-11114
    • Shattil, S.J.1    Hoxie, J.A.2    Cunningham, M.3    Brass, L.F.4
  • 31
    • 0014321756 scopus 로고
    • Genetics of somatic mammalian cells, VII. Induction and isolation of nutritional mutants in Chinese hamster cells
    • Kao FT, Puck TT, (1968) Genetics of somatic mammalian cells, VII. Induction and isolation of nutritional mutants in Chinese hamster cells. Proc Natl Acad Sci U S A 60: 1275-1281.
    • (1968) Proc Natl Acad Sci U S A , vol.60 , pp. 1275-1281
    • Kao, F.T.1    Puck, T.T.2
  • 32
    • 0023084783 scopus 로고
    • Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system
    • DuBridge RB, Tang P, Hsia HC, Leong PM, Miller JH, et al. (1987) Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system. Mol Cell Biol 7: 379-387.
    • (1987) Mol Cell Biol , vol.7 , pp. 379-387
    • DuBridge, R.B.1    Tang, P.2    Hsia, H.C.3    Leong, P.M.4    Miller, J.H.5
  • 33
    • 84883840386 scopus 로고
    • Quantitative studies of the growth of mouse embryo cells in culture and their development into established lines
    • Todaro GJ, Green H, (1963) Quantitative studies of the growth of mouse embryo cells in culture and their development into established lines. J Cell Biol 17: 299-313.
    • (1963) J Cell Biol , vol.17 , pp. 299-313
    • Todaro, G.J.1    Green, H.2
  • 34
    • 0032170171 scopus 로고    scopus 로고
    • Tetracycline repressor, tetR, rather than the tetR-mammalian cell transcription factor fusion derivatives, regulates inducible gene expression in mammalian cells
    • Yao F, Svensjo T, Winkler T, Lu M, Eriksson C, et al. (1998) Tetracycline repressor, tetR, rather than the tetR-mammalian cell transcription factor fusion derivatives, regulates inducible gene expression in mammalian cells. Hum Gene Ther 9: 1939-1950.
    • (1998) Hum Gene Ther , vol.9 , pp. 1939-1950
    • Yao, F.1    Svensjo, T.2    Winkler, T.3    Lu, M.4    Eriksson, C.5
  • 35
    • 0141865705 scopus 로고    scopus 로고
    • Talin binding to integrin beta tails: a final common step in integrin activation
    • Tadokoro S, Shattil SJ, Eto K, Tai V, Liddington RC, et al. (2003) Talin binding to integrin beta tails: a final common step in integrin activation. Science 302: 103-106.
    • (2003) Science , vol.302 , pp. 103-106
    • Tadokoro, S.1    Shattil, S.J.2    Eto, K.3    Tai, V.4    Liddington, R.C.5
  • 36
    • 0037422583 scopus 로고    scopus 로고
    • Inhibiting HIV-1 infection in human T cells by lentiviral-mediated delivery of small interfering RNA against CCR5
    • Qin XF, An DS, Chen IS, Baltimore D, (2003) Inhibiting HIV-1 infection in human T cells by lentiviral-mediated delivery of small interfering RNA against CCR5. Proc Natl Acad Sci U S A 100: 183-188.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 183-188
    • Qin, X.F.1    An, D.S.2    Chen, I.S.3    Baltimore, D.4
  • 38
    • 23844457919 scopus 로고    scopus 로고
    • Specification of the direction of adhesive signaling by the integrin beta cytoplasmic domain
    • Arias-Salgado EG, Lizano S, Shattil SJ, Ginsberg MH, (2005) Specification of the direction of adhesive signaling by the integrin beta cytoplasmic domain. J Biol Chem 280: 29699-29707.
    • (2005) J Biol Chem , vol.280 , pp. 29699-29707
    • Arias-Salgado, E.G.1    Lizano, S.2    Shattil, S.J.3    Ginsberg, M.H.4
  • 39
    • 0002118130 scopus 로고    scopus 로고
    • Molecular basis for platelet activation
    • In: Hoffman R, Benz E, Shattil S, Furie B, Silberstein L, McGlave P, Heslop H, editors, 5 Ed
    • Brass LF, (2009) Molecular basis for platelet activation. In: Hoffman R, Benz E, Shattil S, Furie B, Silberstein L, McGlave P, Heslop H, editors. Hematology. Basic Principles and Practice pp. 1793-1803 5 Ed.
    • (2009) Hematology. Basic Principles and Practice , pp. 1793-1803
    • Brass, L.F.1
  • 40
    • 70349309642 scopus 로고    scopus 로고
    • How ILK and kindlins cooperate to orchestrate integrin signaling
    • Bottcher RT, Lange A, Fassler R, (2009) How ILK and kindlins cooperate to orchestrate integrin signaling. Curr Opin Cell Biol 21: 670-675.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 670-675
    • Bottcher, R.T.1    Lange, A.2    Fassler, R.3
  • 41
    • 77957269801 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of integrin beta3 regulates kindlin-2 binding and integrin activation
    • Bledzka K, Bialkowska K, Nie H, Qin J, Byzova T, et al. (2010) Tyrosine phosphorylation of integrin beta3 regulates kindlin-2 binding and integrin activation. J Biol Chem 285: 30370-30374.
    • (2010) J Biol Chem , vol.285 , pp. 30370-30374
    • Bledzka, K.1    Bialkowska, K.2    Nie, H.3    Qin, J.4    Byzova, T.5
  • 42
  • 43
    • 84872115717 scopus 로고    scopus 로고
    • Pleckstrin homology (PH) domains and phosphoinositides
    • Lemmon MA, (2007) Pleckstrin homology (PH) domains and phosphoinositides. Biochem Soc Symp pp. 81-93.
    • (2007) Biochem Soc Symp , pp. 81-93
    • Lemmon, M.A.1
  • 44
    • 79952802913 scopus 로고    scopus 로고
    • Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins
    • Qu H, Tu Y, Shi X, Larjava H, Saleem MA, et al. (2011) Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins. J Cell Sci 124: 879-891.
    • (2011) J Cell Sci , vol.124 , pp. 879-891
    • Qu, H.1    Tu, Y.2    Shi, X.3    Larjava, H.4    Saleem, M.A.5
  • 45
    • 0024336139 scopus 로고
    • Efficient surface expression of platelet GPIIb-IIIa requires both subunits
    • O'Toole TE, Loftus JC, Plow EF, Glass AA, Harper JR, et al. (1989) Efficient surface expression of platelet GPIIb-IIIa requires both subunits. Blood 74: 14-18.
    • (1989) Blood , vol.74 , pp. 14-18
    • O'Toole, T.E.1    Loftus, J.C.2    Plow, E.F.3    Glass, A.A.4    Harper, J.R.5
  • 46
    • 78751684506 scopus 로고    scopus 로고
    • High-throughput sequencing identifies STAT3 as the DNA-associated factor for p53-NF-kappaB-complex-dependent gene expression in human heart failure
    • Choy MK, Movassagh M, Siggens L, Vujic A, Goddard M, et al. (2010) High-throughput sequencing identifies STAT3 as the DNA-associated factor for p53-NF-kappaB-complex-dependent gene expression in human heart failure. Genome Med 2: 37.
    • (2010) Genome Med , vol.2 , pp. 37
    • Choy, M.K.1    Movassagh, M.2    Siggens, L.3    Vujic, A.4    Goddard, M.5
  • 47
    • 78149474027 scopus 로고    scopus 로고
    • ErbB/HER receptor activation and preclinical efficacy of lapatinib in vestibular schwannoma
    • Ammoun S, Cunliffe CH, Allen JC, Chiriboga L, Giancotti FG, et al. (2010) ErbB/HER receptor activation and preclinical efficacy of lapatinib in vestibular schwannoma. Neuro Oncol 12: 834-843.
    • (2010) Neuro Oncol , vol.12 , pp. 834-843
    • Ammoun, S.1    Cunliffe, C.H.2    Allen, J.C.3    Chiriboga, L.4    Giancotti, F.G.5
  • 48
    • 48049095013 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation (BiFC) analysis of protein interactions in Caenorhabditis elegans
    • Hiatt SM, Shyu YJ, Duren HM, Hu CD, (2008) Bimolecular fluorescence complementation (BiFC) analysis of protein interactions in Caenorhabditis elegans. Methods 45: 185-191.
    • (2008) Methods , vol.45 , pp. 185-191
    • Hiatt, S.M.1    Shyu, Y.J.2    Duren, H.M.3    Hu, C.D.4
  • 49
    • 37249010179 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation: visualization of molecular interactions in living cells
    • Kerppola TK, (2008) Bimolecular fluorescence complementation: visualization of molecular interactions in living cells. Methods Cell Biol 85: 431-470.
    • (2008) Methods Cell Biol , vol.85 , pp. 431-470
    • Kerppola, T.K.1
  • 50
    • 78349235354 scopus 로고    scopus 로고
    • An improved bimolecular fluorescence complementation assay with a high signal-to-noise ratio
    • Kodama Y, Hu CD, (2010) An improved bimolecular fluorescence complementation assay with a high signal-to-noise ratio. Biotechniques 49: 793-805.
    • (2010) Biotechniques , vol.49 , pp. 793-805
    • Kodama, Y.1    Hu, C.D.2
  • 51
    • 0033213922 scopus 로고    scopus 로고
    • The Talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation
    • Calderwood DA, Zent R, Grant R, Rees DJ, Hynes RO, et al. (1999) The Talin head domain binds to integrin beta 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
  • 52
    • 84857735762 scopus 로고    scopus 로고
    • A conserved lipid-binding loop in the Kindlin FERM F1 domain is required for Kindlin-mediated alphaIIbbeta3 integrin Co-activation
    • in press
    • Bouaouina M, Goult BT, Huet-Calderwood C, Bate N, Brahme NN, et al. (2012) A conserved lipid-binding loop in the Kindlin FERM F1 domain is required for Kindlin-mediated alphaIIbbeta3 integrin Co-activation. J Biol Chem in press.
    • (2012) J Biol Chem
    • Bouaouina, M.1    Goult, B.T.2    Huet-Calderwood, C.3    Bate, N.4    Brahme, N.N.5
  • 53
    • 80855133531 scopus 로고    scopus 로고
    • Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation
    • Perera HD, Ma YQ, Yang J, Hirbawi J, Plow EF, et al. (2011) Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation. Structure 19: 1664-1671.
    • (2011) Structure , vol.19 , pp. 1664-1671
    • Perera, H.D.1    Ma, Y.Q.2    Yang, J.3    Hirbawi, J.4    Plow, E.F.5
  • 54
    • 77953317401 scopus 로고    scopus 로고
    • The integrin co-activator Kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell
    • Bialkowska K, Ma YQ, Bledzka K, Sossey-Alaoui K, Izem L, et al. (2010) The integrin co-activator Kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell. J Biol Chem 285: 18640-18649.
    • (2010) J Biol Chem , vol.285 , pp. 18640-18649
    • Bialkowska, K.1    Ma, Y.Q.2    Bledzka, K.3    Sossey-Alaoui, K.4    Izem, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.