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Volumn 8, Issue 2, 2013, Pages

A Role of Kindlin-3 in Integrin αMβ2 Outside-In Signaling and the Syk-Vav1-Rac1/Cdc42 Signaling Axis

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; INTEGRIN; INTEGRIN ALPHAMBETA2; KINDLIN 3; PROTEIN CDC42; PROTEIN KINASE SYK; PROTEIN VAV1; RAC1 PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; VAV PROTEIN;

EID: 84874282556     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0056911     Document Type: Article
Times cited : (30)

References (80)
  • 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
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics of integrin-based cell adhesion
    • Arnaout MA, Goodman SL, Xiong JP, (2007) Structure and mechanics of integrin-based cell adhesion. Curr Opin Cell Biol 19: 495-507.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 495-507
    • Arnaout, M.A.1    Goodman, S.L.2    Xiong, J.P.3
  • 3
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo BH, Carman CV, Springer TA, (2007) Structural basis of integrin regulation and signaling. Annu Rev Immunol 25: 619-647.
    • (2007) Annu Rev Immunol , vol.25 , pp. 619-647
    • Luo, B.H.1    Carman, C.V.2    Springer, T.A.3
  • 5
    • 65649146879 scopus 로고    scopus 로고
    • The mechanical integrin cycle
    • Puklin-Faucher E, Sheetz MP, (2009) The mechanical integrin cycle. J Cell Sci 122: 179-186.
    • (2009) J Cell Sci , vol.122 , pp. 179-186
    • Puklin-Faucher, E.1    Sheetz, M.P.2
  • 6
    • 34548745249 scopus 로고    scopus 로고
    • A catch to integrin activation
    • McEver RP, Zhu C, (2007) A catch to integrin activation. Nat Immunol 8: 1035-1037.
    • (2007) Nat Immunol , vol.8 , pp. 1035-1037
    • McEver, R.P.1    Zhu, C.2
  • 7
    • 84859475497 scopus 로고    scopus 로고
    • The leucocyte β2 (CD18) integrins: the structure, functional regulation and signalling properties
    • Tan SM, (2012) The leucocyte β2 (CD18) integrins: the structure, functional regulation and signalling properties. Bioscience Reports 32: 241-269.
    • (2012) Bioscience Reports , vol.32 , pp. 241-269
    • Tan, S.M.1
  • 8
    • 0025195764 scopus 로고
    • Structure and function of leukocyte integrins
    • Larson RS, Springer TA, (1990) Structure and function of leukocyte integrins. Immunol Rev 114: 181-217.
    • (1990) Immunol Rev , vol.114 , pp. 181-217
    • Larson, R.S.1    Springer, T.A.2
  • 9
    • 34548416749 scopus 로고    scopus 로고
    • Differential regulation of CD11b on γδ T cells and monocytes in response to unripe apple polyphenols
    • Graff JC, Jutila MA, (2007) Differential regulation of CD11b on γδ T cells and monocytes in response to unripe apple polyphenols. J Leukoc Biol 82: 603-607.
    • (2007) J Leukoc Biol , vol.82 , pp. 603-607
    • Graff, J.C.1    Jutila, M.A.2
  • 10
    • 0018758819 scopus 로고
    • Mac-1: a macrophage differentiation antigen identified by monoclonal antibody
    • Springer T, Galfre G, Secher DS, Milstein C, (1979) Mac-1: a macrophage differentiation antigen identified by monoclonal antibody. Eur J Immunol 9: 301-306.
    • (1979) Eur J Immunol , vol.9 , pp. 301-306
    • Springer, T.1    Galfre, G.2    Secher, D.S.3    Milstein, C.4
  • 11
    • 0019953149 scopus 로고
    • Anti-Mac-1 selectively inhibits the mouse and human type three complement receptor
    • Beller DI, Springer TA, Schreiber RD, (1982) Anti-Mac-1 selectively inhibits the mouse and human type three complement receptor. J Exp Med 156: 1000-1009.
    • (1982) J Exp Med , vol.156 , pp. 1000-1009
    • Beller, D.I.1    Springer, T.A.2    Schreiber, R.D.3
  • 12
    • 0020563394 scopus 로고
    • Inhibition of phagocytosis of complement C3- or immunoglobulin G-coated particles and of C3bi binding by monoclonal antibodies to a monocyte-granulocyte membrane glycoprotein (Mol)
    • Arnaout MA, Todd RF, Dana N, Melamed J, Schlossman SF, et al. (1983) Inhibition of phagocytosis of complement C3- or immunoglobulin G-coated particles and of C3bi binding by monoclonal antibodies to a monocyte-granulocyte membrane glycoprotein (Mol). J Clin Invest 72: 171-179.
    • (1983) J Clin Invest , vol.72 , pp. 171-179
    • Arnaout, M.A.1    Todd, R.F.2    Dana, N.3    Melamed, J.4    Schlossman, S.F.5
  • 13
    • 0032729875 scopus 로고    scopus 로고
    • Relative contribution of LFA-1 and Mac-1 to neutrophil adhesion and migration
    • Ding ZM, Babensee JE, Simon SI, Lu H, Perrard JL, et al. (1999) Relative contribution of LFA-1 and Mac-1 to neutrophil adhesion and migration. J Immunol 163: 5029-5038.
    • (1999) J Immunol , vol.163 , pp. 5029-5038
    • Ding, Z.M.1    Babensee, J.E.2    Simon, S.I.3    Lu, H.4    Perrard, J.L.5
  • 14
    • 10744229528 scopus 로고    scopus 로고
    • The pattern recognition receptor (RAGE) is a counterreceptor for leukocyte integrins: a novel pathway for inflammatory cell recruitment
    • Chavakis T, Bierhaus A, Al-Fakhri N, Schneider D, Witte S, et al. (2003) The pattern recognition receptor (RAGE) is a counterreceptor for leukocyte integrins: a novel pathway for inflammatory cell recruitment. J Exp Med 198: 1507-1515.
    • (2003) J Exp Med , vol.198 , pp. 1507-1515
    • Chavakis, T.1    Bierhaus, A.2    Al-Fakhri, N.3    Schneider, D.4    Witte, S.5
  • 15
    • 4043073635 scopus 로고    scopus 로고
    • Integrin engagement regulates monocyte differentiation through the forkhead transcription factor Foxp1
    • Shi C, Zhang X, Chen Z, Sulaiman K, Feinberg MW, et al. (2004) Integrin engagement regulates monocyte differentiation through the forkhead transcription factor Foxp1. J Clin Invest 114: 408-418.
    • (2004) J Clin Invest , vol.114 , pp. 408-418
    • Shi, C.1    Zhang, X.2    Chen, Z.3    Sulaiman, K.4    Feinberg, M.W.5
  • 16
    • 58149386502 scopus 로고    scopus 로고
    • Down-regulation of the forkhead transcription factor Foxp1 is required for monocyte differentiation and macrophage function
    • Shi C, Sakuma M, Mooroka T, Liscoe A, Gao H, et al. (2008) Down-regulation of the forkhead transcription factor Foxp1 is required for monocyte differentiation and macrophage function. Blood 112: 4699-4711.
    • (2008) Blood , vol.112 , pp. 4699-4711
    • Shi, C.1    Sakuma, M.2    Mooroka, T.3    Liscoe, A.4    Gao, H.5
  • 17
    • 77951629952 scopus 로고    scopus 로고
    • Integrin αMβ2 clustering triggers phosphorylation and activation of protein kinase Cδ that regulates transcription factor Foxp1 expression in monocytes
    • Xue ZH, Zhao CQ, Chua GL, Tan SW, Tang XY, et al. (2010) Integrin αMβ2 clustering triggers phosphorylation and activation of protein kinase Cδ that regulates transcription factor Foxp1 expression in monocytes. J Immunol 184: 3697-3709.
    • (2010) J Immunol , vol.184 , pp. 3697-3709
    • Xue, Z.H.1    Zhao, C.Q.2    Chua, G.L.3    Tan, S.W.4    Tang, X.Y.5
  • 18
    • 20644444103 scopus 로고    scopus 로고
    • Neutrophil β2 integrins: moderators of life or death decisions
    • Mayadas TN, Cullere X, (2005) Neutrophil β2 integrins: moderators of life or death decisions. Trends Immunol 26: 388-395.
    • (2005) Trends Immunol , vol.26 , pp. 388-395
    • Mayadas, T.N.1    Cullere, X.2
  • 19
    • 33746618323 scopus 로고    scopus 로고
    • The apoptotic-cell receptor CR3, but not αVβ5, is a regulator of human dendritic-cell immunostimulatory function
    • Skoberne M, Somersan S, Almodovar W, Truong T, Petrova K, et al. (2006) The apoptotic-cell receptor CR3, but not αVβ5, is a regulator of human dendritic-cell immunostimulatory function. Blood 108: 947-955.
    • (2006) Blood , vol.108 , pp. 947-955
    • Skoberne, M.1    Somersan, S.2    Almodovar, W.3    Truong, T.4    Petrova, K.5
  • 20
    • 77954946392 scopus 로고    scopus 로고
    • Integrin CD11b negatively regulates TLR-triggered inflammatory responses by activating Syk and promoting degradation of MyD88 and TRIF via Cbl-b
    • Han C, Jin J, Xu S, Liu H, Li N, et al. (2010) Integrin CD11b negatively regulates TLR-triggered inflammatory responses by activating Syk and promoting degradation of MyD88 and TRIF via Cbl-b. Nat Immunol 11: 734-742.
    • (2010) Nat Immunol , vol.11 , pp. 734-742
    • Han, C.1    Jin, J.2    Xu, S.3    Liu, H.4    Li, N.5
  • 21
    • 0141865705 scopus 로고    scopus 로고
    • Talin binding to integrin β 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 β 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
  • 23
    • 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
  • 24
    • 70349312643 scopus 로고    scopus 로고
    • The Kindlin protein family: new members to the club of focal adhesion proteins
    • Meves A, Stremmel C, Gottschalk K, Fassler R, (2009) The Kindlin protein family: new members to the club of focal adhesion proteins. Trends Cell Biol 19: 504-513.
    • (2009) Trends Cell Biol , vol.19 , pp. 504-513
    • Meves, A.1    Stremmel, C.2    Gottschalk, K.3    Fassler, R.4
  • 25
  • 26
    • 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
  • 27
    • 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
  • 28
    • 55249083592 scopus 로고    scopus 로고
    • Kindlin-3: a new gene involved in the pathogenesis of LAD-III
    • Mory A, Feigelson SW, Yarali N, Kilic SS, Bayhan GI, et al. (2008) Kindlin-3: a new gene involved in the pathogenesis of LAD-III. Blood 112: 2591.
    • (2008) Blood , vol.112 , pp. 2591
    • Mory, A.1    Feigelson, S.W.2    Yarali, N.3    Kilic, S.S.4    Bayhan, G.I.5
  • 29
    • 61949240364 scopus 로고    scopus 로고
    • A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans
    • Malinin NL, Zhang L, Choi J, Ciocea A, Razorenova O, et al. (2009) A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans. Nat Med 15: 313-318.
    • (2009) Nat Med , vol.15 , pp. 313-318
    • Malinin, N.L.1    Zhang, L.2    Choi, J.3    Ciocea, A.4    Razorenova, O.5
  • 30
    • 61949352480 scopus 로고    scopus 로고
    • Kindlin-3 is required for β2 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 β2 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
  • 31
    • 61949086409 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation
    • Svensson L, Howarth K, McDowall A, Patzak I, Evans R, et al. (2009) Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation. Nat Med 15: 306-312.
    • (2009) Nat Med , vol.15 , pp. 306-312
    • Svensson, L.1    Howarth, K.2    McDowall, A.3    Patzak, I.4    Evans, R.5
  • 32
    • 77954755706 scopus 로고    scopus 로고
    • Two mutations in the KINDLIN3 gene of a new leukocyte adhesion deficiency III patient reveal distinct effects on leukocyte function in vitro
    • McDowall A, Svensson L, Stanley P, Patzak I, Chakravarty P, et al. (2010) Two mutations in the KINDLIN3 gene of a new leukocyte adhesion deficiency III patient reveal distinct effects on leukocyte function in vitro. Blood 115: 4834-4842.
    • (2010) Blood , vol.115 , pp. 4834-4842
    • McDowall, A.1    Svensson, L.2    Stanley, P.3    Patzak, I.4    Chakravarty, P.5
  • 33
    • 70449674210 scopus 로고    scopus 로고
    • The structure of the N-terminus of kindlin-1: a domain important for αIIbβ3 integrin activation
    • Goult BT, Bouaouina M, Harburger DS, Bate N, Patel B, et al. (2009) The structure of the N-terminus of kindlin-1: a domain important for αIIbβ3 integrin activation. J Mol Biol 394: 944-956.
    • (2009) J Mol Biol , vol.394 , pp. 944-956
    • Goult, B.T.1    Bouaouina, M.2    Harburger, D.S.3    Bate, N.4    Patel, B.5
  • 34
    • 84857735762 scopus 로고    scopus 로고
    • A conserved lipid-binding loop in the kindlin FERM F1 domain is required for kindlin-mediated αIIbβ3 integrin co-activation
    • 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 αIIbβ3 integrin co-activation. J Biol Chem 287: 6979-6990.
    • (2012) J Biol Chem , vol.287 , pp. 6979-6990
    • Bouaouina, M.1    Goult, B.T.2    Huet-Calderwood, C.3    Bate, N.4    Brahme, N.N.5
  • 35
    • 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
  • 36
    • 83355174039 scopus 로고    scopus 로고
    • Structural basis of phosphoinositide binding to kindlin-2 protein pleckstrin homology domain in regulating integrin activation
    • Liu J, Fukuda K, Xu Z, Ma YQ, Hirbawi J, et al. (2011) Structural basis of phosphoinositide binding to kindlin-2 protein pleckstrin homology domain in regulating integrin activation. J Biol Chem 286: 43334-43342.
    • (2011) J Biol Chem , vol.286 , pp. 43334-43342
    • Liu, J.1    Fukuda, K.2    Xu, Z.3    Ma, Y.Q.4    Hirbawi, J.5
  • 37
    • 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
  • 38
    • 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
  • 39
    • 66449119343 scopus 로고    scopus 로고
    • Kindlin-1 and -2 directly bind the C-terminal region of β 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 β 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
  • 40
    • 44149105411 scopus 로고    scopus 로고
    • Kindlin-2 controls bidirectional signaling of integrins
    • Montanez E, Ussar S, Schifferer M, Bosl M, Zent R, et al. (2008) Kindlin-2 controls bidirectional signaling of integrins. Genes Dev 22: 1325-1330.
    • (2008) Genes Dev , vol.22 , pp. 1325-1330
    • Montanez, E.1    Ussar, S.2    Schifferer, M.3    Bosl, M.4    Zent, R.5
  • 41
    • 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
  • 42
    • 84859508096 scopus 로고    scopus 로고
    • Kindlin-3 mediates integrin αLβ2 outside-in signaling, and it interacts with scaffold protein receptor for activated-C kinase 1 (RACK1)
    • Feng C, Li YF, Yau YH, Lee HS, Tang XY, et al. (2012) Kindlin-3 mediates integrin αLβ2 outside-in signaling, and it interacts with scaffold protein receptor for activated-C kinase 1 (RACK1). J Biol Chem 287: 10714-10726.
    • (2012) J Biol Chem , vol.287 , pp. 10714-10726
    • Feng, C.1    Li, Y.F.2    Yau, Y.H.3    Lee, H.S.4    Tang, X.Y.5
  • 43
    • 84864884471 scopus 로고    scopus 로고
    • Kindlin 2 forms a transcriptional complex with β-catenin and TCF4 to enhance Wnt signalling
    • Yu Y, Wu J, Wang Y, Zhao T, Ma B, et al. (2012) Kindlin 2 forms a transcriptional complex with β-catenin and TCF4 to enhance Wnt signalling. EMBO reports 13: 750-758.
    • (2012) EMBO Reports , vol.13 , pp. 750-758
    • Yu, Y.1    Wu, J.2    Wang, Y.3    Zhao, T.4    Ma, B.5
  • 45
    • 73549105028 scopus 로고    scopus 로고
    • Kindlin-1 is required for RhoGTPase-mediated lamellipodia formation in keratinocytes
    • Has C, Herz C, Zimina E, Qu HY, He Y, et al. (2009) Kindlin-1 is required for RhoGTPase-mediated lamellipodia formation in keratinocytes. Am J Pathol 175: 1442-1452.
    • (2009) Am J Pathol , vol.175 , pp. 1442-1452
    • Has, C.1    Herz, C.2    Zimina, E.3    Qu, H.Y.4    He, Y.5
  • 46
    • 84860390299 scopus 로고    scopus 로고
    • Mediation of Rac1 activation by kindlin-2: an essential function in osteoblast adhesion, spreading, and proliferation
    • Jung GY, Park YJ, Han JS, (2011) Mediation of Rac1 activation by kindlin-2: an essential function in osteoblast adhesion, spreading, and proliferation. J Cell Biochem 112: 2541-2548.
    • (2011) J Cell Biochem , vol.112 , pp. 2541-2548
    • Jung, G.Y.1    Park, Y.J.2    Han, J.S.3
  • 47
    • 70349565999 scopus 로고    scopus 로고
    • Loss of kindlin-3 in LAD-III eliminates LFA-1 but not VLA-4 adhesiveness developed under shear flow conditions
    • Manevich-Mendelson E, Feigelson SW, Pasvolsky R, Aker M, Grabovsky V, et al. (2009) Loss of kindlin-3 in LAD-III eliminates LFA-1 but not VLA-4 adhesiveness developed under shear flow conditions. Blood 114: 2344-2353.
    • (2009) Blood , vol.114 , pp. 2344-2353
    • Manevich-Mendelson, E.1    Feigelson, S.W.2    Pasvolsky, R.3    Aker, M.4    Grabovsky, V.5
  • 48
    • 33747174596 scopus 로고    scopus 로고
    • Down-regulation of integrin αMβ2 ligand-binding function by the urokinase-type plasminogen activator receptor
    • Tang ML, Kong LS, Law SK, Tan SM, (2006) Down-regulation of integrin αMβ2 ligand-binding function by the urokinase-type plasminogen activator receptor. Biochem Biophys Res Commun 348: 1184-1193.
    • (2006) Biochem Biophys Res Commun , vol.348 , pp. 1184-1193
    • Tang, M.L.1    Kong, L.S.2    Law, S.K.3    Tan, S.M.4
  • 49
    • 0029620240 scopus 로고
    • KIM127, an antibody that promotes adhesion, maps to a region of CD18 that includes cysteine-rich repeats
    • Stephens P, Romer JT, Spitali M, Shock A, Ortlepp S, et al. (1995) KIM127, an antibody that promotes adhesion, maps to a region of CD18 that includes cysteine-rich repeats. Cell Adhes Commun 3: 375-384.
    • (1995) Cell Adhes Commun , vol.3 , pp. 375-384
    • Stephens, P.1    Romer, J.T.2    Spitali, M.3    Shock, A.4    Ortlepp, S.5
  • 50
    • 0036220127 scopus 로고    scopus 로고
    • Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation
    • Beglova N, Blacklow SC, Takagi J, Springer TA, (2002) Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation. Nat Struct Biol 9: 282-287.
    • (2002) Nat Struct Biol , vol.9 , pp. 282-287
    • Beglova, N.1    Blacklow, S.C.2    Takagi, J.3    Springer, T.A.4
  • 51
    • 0038448143 scopus 로고    scopus 로고
    • Modulation of CD11b/CD18 adhesive activity by its extracellular, membrane-proximal regions
    • Xiong YM, Chen J, Zhang L, (2003) Modulation of CD11b/CD18 adhesive activity by its extracellular, membrane-proximal regions. J Immunol 171: 1042-1050.
    • (2003) J Immunol , vol.171 , pp. 1042-1050
    • Xiong, Y.M.1    Chen, J.2    Zhang, L.3
  • 52
    • 34547106059 scopus 로고    scopus 로고
    • Mutation of a conserved asparagine in the I-like domain promotes constitutively active integrins αLβ2 and αIIbβ3
    • Cheng M, Foo SY, Shi ML, Tang RH, Kong LS, et al. (2007) Mutation of a conserved asparagine in the I-like domain promotes constitutively active integrins αLβ2 and αIIbβ3. J Biol Chem 282: 18225-18232.
    • (2007) J Biol Chem , vol.282 , pp. 18225-18232
    • Cheng, M.1    Foo, S.Y.2    Shi, M.L.3    Tang, R.H.4    Kong, L.S.5
  • 53
    • 44449139065 scopus 로고    scopus 로고
    • Intercellular adhesion molecule-3 binding of integrin αLβ2 requires both extension and opening of the integrin headpiece
    • Tang XY, Li YF, Tan SM, (2008) Intercellular adhesion molecule-3 binding of integrin αLβ2 requires both extension and opening of the integrin headpiece. J Immunol 180: 4793-4804.
    • (2008) J Immunol , vol.180 , pp. 4793-4804
    • Tang, X.Y.1    Li, Y.F.2    Tan, S.M.3
  • 55
    • 33846295127 scopus 로고    scopus 로고
    • Integrin signaling in neutrophils and macrophages uses adaptors containing immunoreceptor tyrosine-based activation motifs
    • Mocsai A, Abram CL, Jakus Z, Hu Y, Lanier LL, et al. (2006) Integrin signaling in neutrophils and macrophages uses adaptors containing immunoreceptor tyrosine-based activation motifs. Nat Immunol 7: 1326-1333.
    • (2006) Nat Immunol , vol.7 , pp. 1326-1333
    • Mocsai, A.1    Abram, C.L.2    Jakus, Z.3    Hu, Y.4    Lanier, L.L.5
  • 56
    • 0027226327 scopus 로고
    • KIM185, a monoclonal antibody to CD18 which induces a change in the conformation of CD18 and promotes both LFA-1- and CR3-dependent adhesion
    • Andrew D, Shock A, Ball E, Ortlepp S, Bell J, et al. (1993) KIM185, a monoclonal antibody to CD18 which induces a change in the conformation of CD18 and promotes both LFA-1- and CR3-dependent adhesion. Eur J Immunol 23: 2217-2222.
    • (1993) Eur J Immunol , vol.23 , pp. 2217-2222
    • Andrew, D.1    Shock, A.2    Ball, E.3    Ortlepp, S.4    Bell, J.5
  • 57
    • 0026736029 scopus 로고
    • The Mac-1 and p150,95 β2 integrins bind denatured proteins to mediate leukocyte cell-substrate adhesion
    • Davis GE, (1992) The Mac-1 and p150,95 β2 integrins bind denatured proteins to mediate leukocyte cell-substrate adhesion. Exp Cell Res 200: 242-252.
    • (1992) Exp Cell Res , vol.200 , pp. 242-252
    • Davis, G.E.1
  • 58
    • 0034283664 scopus 로고    scopus 로고
    • Effect of integrin β2 subunit truncations on LFA-1 (CD11a/CD18) and Mac-1 (CD11b/CD18) assembly, surface expression, and function
    • Tan SM, Hyland RH, Al-Shamkhani A, Douglass WA, Shaw JM, et al. (2000) Effect of integrin β2 subunit truncations on LFA-1 (CD11a/CD18) and Mac-1 (CD11b/CD18) assembly, surface expression, and function. J Immunol 165: 2574-2581.
    • (2000) J Immunol , vol.165 , pp. 2574-2581
    • Tan, S.M.1    Hyland, R.H.2    Al-Shamkhani, A.3    Douglass, W.A.4    Shaw, J.M.5
  • 59
    • 0034783368 scopus 로고    scopus 로고
    • Characterization of four CD18 mutants in leucocyte adhesion deficient (LAD) patients with differential capacities to support expression and function of the CD11/CD18 integrins LFA-1, Mac-1 and p150,95
    • Shaw JM, Al-Shamkhani A, Boxer LA, Buckley CD, Dodds AW, et al. (2001) Characterization of four CD18 mutants in leucocyte adhesion deficient (LAD) patients with differential capacities to support expression and function of the CD11/CD18 integrins LFA-1, Mac-1 and p150,95. Clin Exp Immunol 126: 311-318.
    • (2001) Clin Exp Immunol , vol.126 , pp. 311-318
    • Shaw, J.M.1    Al-Shamkhani, A.2    Boxer, L.A.3    Buckley, C.D.4    Dodds, A.W.5
  • 60
    • 0030499383 scopus 로고    scopus 로고
    • Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product
    • Deckert M, Tartare-Deckert S, Couture C, Mustelin T, Altman A, (1996) Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product. Immunity 5: 591-604.
    • (1996) Immunity , vol.5 , pp. 591-604
    • Deckert, M.1    Tartare-Deckert, S.2    Couture, C.3    Mustelin, T.4    Altman, A.5
  • 61
    • 0032481142 scopus 로고    scopus 로고
    • Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav1
    • Miranti CK, Leng L, Maschberger P, Brugge JS, Shattil SJ, (1998) Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav1. Current biology: CB 8: 1289-1299.
    • (1998) Current Biology: CB , vol.8 , pp. 1289-1299
    • Miranti, C.K.1    Leng, L.2    Maschberger, P.3    Brugge, J.S.4    Shattil, S.J.5
  • 62
    • 33845268014 scopus 로고    scopus 로고
    • The Vav binding site of the non-receptor tyrosine kinase Syk at Tyr 348 is critical for β2 integrin (CD11/CD18)-mediated neutrophil migration
    • Schymeinsky J, Sindrilaru A, Frommhold D, Sperandio M, Gerstl R, et al. (2006) The Vav binding site of the non-receptor tyrosine kinase Syk at Tyr 348 is critical for β2 integrin (CD11/CD18)-mediated neutrophil migration. Blood 108: 3919-3927.
    • (2006) Blood , vol.108 , pp. 3919-3927
    • Schymeinsky, J.1    Sindrilaru, A.2    Frommhold, D.3    Sperandio, M.4    Gerstl, R.5
  • 63
    • 3342903325 scopus 로고    scopus 로고
    • Vav GEFs are required for β2 integrin-dependent functions of neutrophils
    • Gakidis MA, Cullere X, Olson T, Wilsbacher JL, Zhang B, et al. (2004) Vav GEFs are required for β2 integrin-dependent functions of neutrophils. J Cell Biol 166: 273-282.
    • (2004) J Cell Biol , vol.166 , pp. 273-282
    • Gakidis, M.A.1    Cullere, X.2    Olson, T.3    Wilsbacher, J.L.4    Zhang, B.5
  • 64
    • 0033974061 scopus 로고    scopus 로고
    • Regulatory and signaling properties of the Vav family
    • Bustelo XR, (2000) Regulatory and signaling properties of the Vav family. Mol Cell Biol 20: 1461-1477.
    • (2000) Mol Cell Biol , vol.20 , pp. 1461-1477
    • Bustelo, X.R.1
  • 65
    • 84860830766 scopus 로고    scopus 로고
    • Distinct roles for talin-1 and kindlin-3 in LFA-1 extension and affinity regulation
    • Lefort CT, Rossaint J, Moser M, Petrich BG, Zarbock A, et al. (2012) Distinct roles for talin-1 and kindlin-3 in LFA-1 extension and affinity regulation. Blood 119: 4275-4282.
    • (2012) Blood , vol.119 , pp. 4275-4282
    • Lefort, C.T.1    Rossaint, J.2    Moser, M.3    Petrich, B.G.4    Zarbock, A.5
  • 66
    • 0031568669 scopus 로고    scopus 로고
    • Signaling by adhesion in human neutrophils: activation of the p72syk tyrosine kinase and formation of protein complexes containing p72syk and Src family kinases in neutrophils spreading over fibrinogen
    • Yan SR, Huang M, Berton G, (1997) Signaling by adhesion in human neutrophils: activation of the p72syk tyrosine kinase and formation of protein complexes containing p72syk and Src family kinases in neutrophils spreading over fibrinogen. J Immunol 158: 1902-1910.
    • (1997) J Immunol , vol.158 , pp. 1902-1910
    • Yan, S.R.1    Huang, M.2    Berton, G.3
  • 71
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A, (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70: 401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 72
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley AJ, Hall A, (1992) The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70: 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 73
    • 0037799270 scopus 로고    scopus 로고
    • Ligand-dependent activation of integrin αvβ3
    • Butler B, Williams MP, Blystone SD, (2003) Ligand-dependent activation of integrin αvβ3. J Biol Chem 278: 5264-5270.
    • (2003) J Biol Chem , vol.278 , pp. 5264-5270
    • Butler, B.1    Williams, M.P.2    Blystone, S.D.3
  • 74
    • 0037092520 scopus 로고    scopus 로고
    • Differential regulation of Rho GTPases by β1 and β3 integrins: the role of an extracellular domain of integrin in intracellular signaling
    • Miao H, Li S, Hu YL, Yuan S, Zhao Y, et al. (2002) Differential regulation of Rho GTPases by β1 and β3 integrins: the role of an extracellular domain of integrin in intracellular signaling. J Cell Sci 115: 2199-2206.
    • (2002) J Cell Sci , vol.115 , pp. 2199-2206
    • Miao, H.1    Li, S.2    Hu, Y.L.3    Yuan, S.4    Zhao, Y.5
  • 75
    • 33746658154 scopus 로고    scopus 로고
    • FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling
    • Ohta Y, Hartwig JH, Stossel TP, (2006) FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling. Nat Cell Biol 8: 803-814.
    • (2006) Nat Cell Biol , vol.8 , pp. 803-814
    • Ohta, Y.1    Hartwig, J.H.2    Stossel, T.P.3
  • 76
  • 77
    • 66849101632 scopus 로고    scopus 로고
    • Adhesion signaling - crosstalk between integrins, Src and Rho
    • Huveneers S, Danen EH, (2009) Adhesion signaling- crosstalk between integrins, Src and Rho. J Cell Sci 122: 1059-1069.
    • (2009) J Cell Sci , vol.122 , pp. 1059-1069
    • Huveneers, S.1    Danen, E.H.2
  • 78
    • 0037329051 scopus 로고    scopus 로고
    • RACK1 regulates integrin-mediated adhesion, protrusion, and chemotactic cell migration via its Src-binding site
    • Cox EA, Bennin D, Doan AT, O'Toole T, Huttenlocher A, (2003) RACK1 regulates integrin-mediated adhesion, protrusion, and chemotactic cell migration via its Src-binding site. Mol Biol Cell 14: 658-669.
    • (2003) Mol Biol Cell , vol.14 , pp. 658-669
    • Cox, E.A.1    Bennin, D.2    Doan, A.T.3    O'Toole, T.4    Huttenlocher, A.5
  • 79
    • 34347230464 scopus 로고    scopus 로고
    • RACK1 regulates Src activity and modulates paxillin dynamics during cell migration
    • Doan AT, Huttenlocher A, (2007) RACK1 regulates Src activity and modulates paxillin dynamics during cell migration. Exp Cell Res 313: 2667-2679.
    • (2007) Exp Cell Res , vol.313 , pp. 2667-2679
    • Doan, A.T.1    Huttenlocher, A.2
  • 80
    • 2542477014 scopus 로고    scopus 로고
    • RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers
    • de Hoog CL, Foster LJ, Mann M, (2004) RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers. Cell 117: 649-662.
    • (2004) Cell , vol.117 , pp. 649-662
    • de Hoog, C.L.1    Foster, L.J.2    Mann, M.3


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