메뉴 건너뛰기




Volumn 18, Issue 5, 2011, Pages 356-360

Kindlin: Helper, co-activator, or booster of talin in integrin activation?

Author keywords

integrin; kindlin; talin

Indexed keywords

INTEGRIN; INTEGRIN ALPHA2B BETA3; PHOSPHOPROTEIN; PROTEIN KINDLIN; PROTEIN KINDLIN 1; PROTEIN KINDLIN 2; PROTEIN KINDLIN 3; SCAFFOLD PROTEIN; TALIN; UNCLASSIFIED DRUG;

EID: 80051802621     PISSN: 10656251     EISSN: 15317048     Source Type: Journal    
DOI: 10.1097/MOH.0b013e3283497f09     Document Type: Review
Times cited : (42)

References (44)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • DOI 10.1016/S0092-8674(02)00971-6
    • Hynes RO. Integrins: bidirectional, allosteric signaling machines. Cell 2002;110:673-687. (Pubitemid 35283958)
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 2
    • 0029763215 scopus 로고    scopus 로고
    • Analysis of GPIIb/IIIa receptor number by quantification of 7E3 binding to human platelets
    • Wagner CL, Mascelli MA, Neblock DS, et al. Analysis of GPIIb/IIIa receptor number by quantification of 7E3 binding to human platelets. Blood 1996;88:907-914. (Pubitemid 26333313)
    • (1996) Blood , vol.88 , Issue.3 , pp. 907-914
    • Wagner, C.L.1    Mascelli, M.A.2    Neblock, D.S.3    Weisman, H.F.4    Coller, B.S.5    Jordan, R.E.6
  • 3
    • 54049152026 scopus 로고    scopus 로고
    • The GPIIb/IIIa (integrin alphaIIbbeta3) odyssey: A technology-driven saga of a receptor with twists, turns, and even a bend
    • Coller BS, Shattil SJ. The GPIIb/IIIa (integrin alphaIIbbeta3) odyssey: a technology-driven saga of a receptor with twists, turns, and even a bend. Blood 2008;112:3011-3025.
    • (2008) Blood , vol.112 , pp. 3011-3025
    • Coller, B.S.1    Shattil, S.J.2
  • 4
    • 0032523064 scopus 로고    scopus 로고
    • Integrin signaling: The platelet paradigm
    • Shattil SJ, Kashiwagi H, Pampori N. Integrin signaling: the platelet paradigm. Blood 1998;91:2645-2657. (Pubitemid 28227512)
    • (1998) Blood , vol.91 , Issue.8 , pp. 2645-2657
    • Shattil, S.J.1    Kashiwagi, H.2    Pampori, N.3
  • 5
    • 4444264392 scopus 로고    scopus 로고
    • Integrins: Dynamic scaffolds for adhesion and signaling in platelets
    • DOI 10.1182/blood-2004-04-1257
    • Shattil SJ, Newman PJ. Integrins: dynamic scaffolds for adhesion and signaling in platelets. Blood 2004;104:1606-1615. (Pubitemid 39202265)
    • (2004) Blood , vol.104 , Issue.6 , pp. 1606-1615
    • Shattil, S.J.1    Newman, P.J.2
  • 6
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser M, Legate KR, Zent R, Fassler R. The tail of integrins, talin, and kindlins. Science 2009;324:895-899.
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4
  • 7
  • 8
    • 67650288199 scopus 로고    scopus 로고
    • Biochemical and structural properties of the integrin-associated cytoskeletal protein talin
    • Critchley DR. Biochemical and structural properties of the integrin-associated cytoskeletal protein talin. Annu Rev Biophys 2009;38:235-254.
    • (2009) Annu Rev Biophys , vol.38 , pp. 235-254
    • Critchley, D.R.1
  • 9
    • 44449148944 scopus 로고    scopus 로고
    • The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate beta1 and beta3 integrins
    • Bouaouina M, Lad Y, Calderwood DA. The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate beta1 and beta3 integrins. J Biol Chem 2008;283:6118-6125.
    • (2008) J Biol Chem , vol.283 , pp. 6118-6125
    • Bouaouina, M.1    Lad, Y.2    Calderwood, D.A.3
  • 10
    • 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, et al. The Talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation. J Biol Chem 1999;274:28071-28074.
    • (1999) J Biol Chem , vol.274 , pp. 28071-28074
    • Calderwood, D.A.1    Zent, R.2    Grant, R.3
  • 11
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • DOI 10.1126/science.1084174
    • Kim M, Carman CV, Springer TA. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 2003;301:1720-1725. (Pubitemid 37174365)
    • (2003) Science , vol.301 , Issue.5640 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 12
    • 0033667594 scopus 로고    scopus 로고
    • Disruption of the talin gene arrests mouse development at the gastrulation stage
    • Monkley SJ, Zhou XH, Kinston SJ, et al. Disruption of the talin gene arrests mouse development at the gastrulation stage. Dev Dyn 2000;219:560-574.
    • (2000) Dev Dyn , vol.219 , pp. 560-574
    • Monkley, S.J.1    Zhou, X.H.2    Kinston, S.J.3
  • 13
    • 37549029679 scopus 로고    scopus 로고
    • Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo
    • Nieswandt B, Moser M, Pleines I, et al. Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo. J Exp Med 2007;204:3113-3118.
    • (2007) J Exp Med , vol.204 , pp. 3113-3118
    • Nieswandt, B.1    Moser, M.2    Pleines, I.3
  • 14
    • 37549064277 scopus 로고    scopus 로고
    • Talin is required for integrinmediated platelet function in hemostasis and thrombosis
    • Petrich BG, Marchese P, Ruggeri ZM, et al. Talin is required for integrinmediated platelet function in hemostasis and thrombosis. J Exp Med 2007;204:3103-3111.
    • (2007) J Exp Med , vol.204 , pp. 3103-3111
    • Petrich, B.G.1    Marchese, P.2    Ruggeri, Z.M.3
  • 15
    • 79551647521 scopus 로고    scopus 로고
    • Talin-dependent integrin activation is required for fibrin clot retraction by platelets
    • Haling JR, Monkley SJ, Critchley DR, Petrich BG. Talin-dependent integrin activation is required for fibrin clot retraction by platelets. Blood 2011;117:1719-1722.
    • (2011) Blood , vol.117 , pp. 1719-1722
    • Haling, J.R.1    Monkley, S.J.2    Critchley, D.R.3    Petrich, B.G.4
  • 18
    • 66449119343 scopus 로고    scopus 로고
    • Kindlin-1 and-2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrinspecific activation effects
    • This article recognized that over-expressed kindlin is inhibitory for β1 integrin and for β3 integrin in some circumstances. The authors suggested a possible scaffold role for kindlin
    • Harburger DS, Bouaouina M, Calderwood DA. Kindlin-1 and-2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrinspecific activation effects. J Biol Chem 2009;284:11485-11497. This article recognized that over-expressed kindlin is inhibitory for β1 integrin and for β3 integrin in some circumstances. The authors suggested a possible scaffold role for kindlin.
    • (2009) J Biol Chem , vol.284 , pp. 11485-11497
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 19
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • DOI 10.1038/nm1722, PII NM1722
    • Moser M, Nieswandt B, Ussar S, et al. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat Med 2008;14:325-330. This is the first article to recognize and establish the role of kindlin in integrin regulation. (Pubitemid 351347914)
    • (2008) Nature Medicine , vol.14 , Issue.3 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fassler, R.5
  • 20
    • 43149085289 scopus 로고    scopus 로고
    • 3 integrins
    • DOI 10.1083/jcb.200710196
    • Ma YQ, Qin J, Wu C, Plow EF. Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J Cell Biol 2008;181:439-446. This article established that kindlin can synergize with THD in activating integrin aIIbb3. (Pubitemid 351645034)
    • (2008) Journal of Cell Biology , vol.181 , Issue.3 , pp. 439-446
    • Ma, Y.-Q.1    Qin, J.2    Wu, C.3    Plow, E.F.4
  • 22
    • 61949352480 scopus 로고    scopus 로고
    • Kindlin-3 is required for beta2 integrin mediated leukocyte adhesion to endothelial cells
    • Moser M, Bauer M, Schmid S, et al. Kindlin-3 is required for beta2 integrin mediated leukocyte adhesion to endothelial cells. Nat Med 2009;15:300-305.
    • (2009) Nat Med , vol.15 , pp. 300-305
    • Moser, M.1    Bauer, M.2    Schmid, S.3
  • 23
    • 79952435385 scopus 로고    scopus 로고
    • Kindlin-3-mediated signaling from multiple integrin classes is required for osteoclast-mediated bone resorption
    • Schmidt S, Nakchbandi I, Ruppert R, et al. Kindlin-3-mediated signaling from multiple integrin classes is required for osteoclast-mediated bone resorption. J Cell Biol 2011;192:883-897.
    • (2011) J Cell Biol , vol.192 , pp. 883-897
    • Schmidt, S.1    Nakchbandi, I.2    Ruppert, R.3
  • 24
    • 66549121768 scopus 로고    scopus 로고
    • LAD-1/variant syndrome is caused by mutations in FERMT3
    • Kuijpers TW, van de Vijver E, Weterman MA, et al. LAD-1/variant syndrome is caused by mutations in FERMT3. Blood 2009;113:4740-4746.
    • (2009) Blood , vol.113 , pp. 4740-4746
    • Kuijpers, T.W.1    Van De Vijver, E.2    Weterman, M.A.3
  • 25
    • 61949240364 scopus 로고    scopus 로고
    • A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans
    • * was the first to show that mutations in kindlin-3 caused integrin activation defects in human patients with leukocyte adhesion deficiency-III
    • *] was the first to show that mutations in kindlin-3 caused integrin activation defects in human patients with leukocyte adhesion deficiency-III.
    • (2009) Nat Med , vol.15 , pp. 313-318
    • Malinin, N.L.1    Zhang, L.2    Choi, J.3
  • 26
    • 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, et al. Two mutations in the KINDLIN3 gene of a new leukocyte adhesion deficiency III patient reveal distinct effects on leukocyte function in vitro. Blood 2010;115:4834-4842.
    • (2010) Blood , vol.115 , pp. 4834-4842
    • McDowall, A.1    Svensson, L.2    Stanley, P.3
  • 27
    • 61949086409 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3 affecting integrin activation
    • * was the first to show that mutations in kindlin-3 caused integrin activation defects in human patients with leukocyte adhesion deficiency-III
    • *] was the first to show that mutations in kindlin-3 caused integrin activation defects in human patients with leukocyte adhesion deficiency-III.
    • (2009) Nat Med , vol.15 , pp. 306-312
    • Svensson, L.1    Howarth, K.2    McDowall, A.3
  • 28
    • 79955538508 scopus 로고    scopus 로고
    • A novel leukocyte adhesion deficiency-III variant: Kindlin-3 deficiency results in integrin and nonintegrin-related defects in different steps of leukocyte adhesion
    • Robert P, Canault M, Farnarier C, et al. A novel leukocyte adhesion deficiency-III variant: kindlin-3 deficiency results in integrin and nonintegrin-related defects in different steps of leukocyte adhesion. J Immunol 2011;186:5273-5283.
    • (2011) J Immunol , vol.186 , pp. 5273-5283
    • Robert, P.1    Canault, M.2    Farnarier, C.3
  • 29
    • 58149154658 scopus 로고    scopus 로고
    • Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction
    • Ussar S, Moser M, Widmaier M, et al. Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction. PLoS Genet 2008;4:e1000289.
    • (2008) PLoS Genet , vol.4
    • Ussar, S.1    Moser, M.2    Widmaier, M.3
  • 31
    • 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, et al. Loss of Kindlin-3 in LAD-III eliminates LFA-1 but not VLA-4 adhesiveness developed under shear flow conditions. Blood 2009;114:2344-2353.
    • (2009) Blood , vol.114 , pp. 2344-2353
    • Manevich-Mendelson, E.1    Feigelson, S.W.2    Pasvolsky, R.3
  • 33
    • 75749154495 scopus 로고    scopus 로고
    • Recreation of the terminal events in physiological integrin activation
    • This study utilizes monomeric integrins embedded in phospholipid nanodiscs to show that the THD alone is sufficient to activate integrins and does not require integrin clustering
    • Ye F, Hu G, Taylor D, et al. Recreation of the terminal events in physiological integrin activation. J Cell Biol 2010;188:157-173. This study utilizes monomeric integrins embedded in phospholipid nanodiscs to show that the THD alone is sufficient to activate integrins and does not require integrin clustering.
    • (2010) J Cell Biol , vol.188 , pp. 157-173
    • Ye, F.1    Hu, G.2    Taylor, D.3
  • 35
    • 79952802913 scopus 로고    scopus 로고
    • Kindlin-2 regulates podocyte adhesion andfibronectin matrix deposition through interactions with phosphoinositides and integrins
    • Qu H, Tu Y, Shi X, et al. Kindlin-2 regulates podocyte adhesion andfibronectin matrix deposition through interactions with phosphoinositides and integrins. J Cell Sci 2011;124(Pt 6):879-891.
    • (2011) J Cell Sci , vol.124 , Issue.6 PART , pp. 879-891
    • Qu, H.1    Tu, Y.2    Shi, X.3
  • 36
    • 43049110021 scopus 로고    scopus 로고
    • The NHL-domain protein Wech is crucial for the integrin-cytoskeleton link
    • Loer B, Bauer R, Bornheim R, et al. The NHL-domain protein Wech is crucial for the integrin-cytoskeleton link. Nat Cell Biol 2008;10:422-428.
    • (2008) Nat Cell Biol , vol.10 , pp. 422-428
    • Loer, B.1    Bauer, R.2    Bornheim, R.3
  • 37
    • 78651109051 scopus 로고    scopus 로고
    • NMR analysis of the alphaIIb beta3 cytoplasmic interaction suggests a mechanism for integrin regulation
    • Metcalf DG, Moore DT, Wu Y, et al. NMR analysis of the alphaIIb beta3 cytoplasmic interaction suggests a mechanism for integrin regulation. Proc Natl Acad Sci USA 2011;107:22481-22486.
    • (2011) Proc Natl Acad Sci USA , vol.107 , pp. 22481-22486
    • Metcalf, D.G.1    Moore, D.T.2    Wu, Y.3
  • 38
    • 77953317401 scopus 로고    scopus 로고
    • The integrin co-activator Kindlin-3 is expressed and functional in a nonhematopoietic cell, the endothelial cell
    • This article showed that kindlin-2 and kindlin-3 might localize differently in cells and display some integrin specificity
    • Bialkowska K, Ma YQ, Bledzka K, et al. The integrin co-activator Kindlin-3 is expressed and functional in a nonhematopoietic cell, the endothelial cell. J Biol Chem 2010;285:18640-18649. This article showed that kindlin-2 and kindlin-3 might localize differently in cells and display some integrin specificity.
    • (2010) J Biol Chem , vol.285 , pp. 18640-18649
    • Bialkowska, K.1    Ma, Y.Q.2    Bledzka, K.3
  • 39
    • 74049126062 scopus 로고    scopus 로고
    • New PI (4, 5) P2-and membrane proximal integrin-binding motifs in the talin head control beta3-integrin clustering
    • Saltel F, Mortier E, Hytonen VP, et al. New PI (4, 5) P2-and membrane proximal integrin-binding motifs in the talin head control beta3-integrin clustering. J Cell Biol 2009;187:715-731.
    • (2009) J Cell Biol , vol.187 , pp. 715-731
    • Saltel, F.1    Mortier, E.2    Hytonen, V.P.3
  • 40
    • 66549097709 scopus 로고    scopus 로고
    • Interactions of platelet integrin alphaIIb and beta3 transmembrane domains in mammalian cell membranes and their role in integrin activation
    • Kim C, Lau TL, Ulmer TS, Ginsberg MH. Interactions of platelet integrin alphaIIb and beta3 transmembrane domains in mammalian cell membranes and their role in integrin activation. Blood 2009;113:4747-4753.
    • (2009) Blood , vol.113 , pp. 4747-4753
    • Kim, C.1    Lau, T.L.2    Ulmer, T.S.3    Ginsberg, M.H.4
  • 42
    • 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 within the rod domain
    • DOI 10.1074/jbc.M400947200
    • Tremuth L, Kreis S, Melchior C, et al. A fluorescence cell biology approach to map the second integrin-binding site of talin to a 130-amino acid sequence within the rod domain. J Biol Chem 2004;279:22258-22266. (Pubitemid 38679422)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.21 , 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
  • 43
    • 0035976972 scopus 로고    scopus 로고
    • Localization of an integrin binding site to the C terminus of talin
    • Xing B, Jedsadayanmata A, Lam SC. Localization of an integrin binding site to the C terminus of talin. J Biol Chem 2001;276:44373-44378.
    • (2001) J Biol Chem , vol.276 , pp. 44373-44378
    • Xing, B.1    Jedsadayanmata, A.2    Lam, S.C.3
  • 44
    • 0028306890 scopus 로고
    • Determinants ofspecificity of a baculovirusexpressed antibody Fab fragment that binds selectively to the activated form of integrin alpha IIb beta 3
    • Abrams C, Deng YJ, Steiner B, et al. Determinants ofspecificity of a baculovirusexpressed antibody Fab fragment that binds selectively to the activated form of integrin alpha IIb beta 3. J Biol Chem 1994;269:18781-18788.
    • (1994) J Biol Chem , vol.269 , pp. 18781-18788
    • Abrams, C.1    Deng, Y.J.2    Steiner, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.