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Volumn 434, Issue 2, 2013, Pages 382-387

Integrity of kindlin-2 FERM subdomains is required for supporting integrin activation

Author keywords

Cell spreading; Integrin activation; Protein protein interaction

Indexed keywords

INTEGRIN; KINDLIN 2; PROTEIN; TALIN; UNCLASSIFIED DRUG;

EID: 84877061239     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.03.086     Document Type: Article
Times cited : (17)

References (40)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 2002, 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 2
    • 57049169143 scopus 로고    scopus 로고
    • Kindlins: essential regulators of integrin signalling and cell-matrix adhesion
    • Larjava H., Plow E.F., Wu C. Kindlins: essential regulators of integrin signalling and cell-matrix adhesion. EMBO Rep. 2008, 9:1203-1208.
    • (2008) EMBO Rep. , vol.9 , pp. 1203-1208
    • Larjava, H.1    Plow, E.F.2    Wu, C.3
  • 3
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser M., Legate K.R., 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
  • 5
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M., Carman C.V., Springer T.A. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 2003, 301:1720-1725.
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 6
    • 16644368209 scopus 로고    scopus 로고
    • Integrin bidirectional signaling: a molecular view
    • Qin J., Vinogradova O., Plow E.F. Integrin bidirectional signaling: a molecular view. PLoS Biol. 2004, 2:e169.
    • (2004) PLoS Biol. , vol.2
    • Qin, J.1    Vinogradova, O.2    Plow, E.F.3
  • 7
    • 34250768894 scopus 로고    scopus 로고
    • Platelet integrin alpha(IIb)beta(3): activation mechanisms
    • Ma Y.Q., Qin J., Plow E.F. Platelet integrin alpha(IIb)beta(3): activation mechanisms. J. Thromb. Haemost. 2007, 5:1345-1352.
    • (2007) J. Thromb. Haemost. , vol.5 , pp. 1345-1352
    • Ma, Y.Q.1    Qin, J.2    Plow, E.F.3
  • 8
    • 0033213922 scopus 로고    scopus 로고
    • The Talin head domain binds to integrin beta subunit cytoplasmic tails and regulates integrin activation
    • Calderwood D.A., Zent R., Grant R., Rees D.J., Hynes R.O., Ginsberg M.H. 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    Rees, D.J.4    Hynes, R.O.5    Ginsberg, M.H.6
  • 10
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin αIIbβ3 "inside-out" activation as regulated by its cytoplasmic face
    • Vinogradova O., Velyvis A., Velyviene A., Hu B., Haas T.A., Plow E.F., Qin J. A structural mechanism of integrin αIIbβ3 "inside-out" activation as regulated by its cytoplasmic face. Cell 2002, 110:587-597.
    • (2002) Cell , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.A.5    Plow, E.F.6    Qin, J.7
  • 14
    • 77953233840 scopus 로고    scopus 로고
    • Kindlins in FERM adhesion
    • Malinin N.L., Plow E.F., Byzova T.V. Kindlins in FERM adhesion. Blood 2010, 115:4011-4017.
    • (2010) Blood , vol.115 , pp. 4011-4017
    • Malinin, N.L.1    Plow, E.F.2    Byzova, T.V.3
  • 15
    • 79960628458 scopus 로고    scopus 로고
    • Molecular mechanism of inside-out integrin regulation
    • Ye F., Kim C., Ginsberg M.H. Molecular mechanism of inside-out integrin regulation. J. Thromb. Haemost. 2011, 9(Suppl. 1):20-25.
    • (2011) J. Thromb. Haemost. , vol.9 , Issue.SUPPL. 1 , pp. 20-25
    • Ye, F.1    Kim, C.2    Ginsberg, M.H.3
  • 16
    • 0028053243 scopus 로고
    • Identification of serum-inducible genes: different patterns of gene regulation during G0->S and G1->S progression
    • Wick M., Burger C., Brusselbach S., Lucibello F.C., Muller R. Identification of serum-inducible genes: different patterns of gene regulation during G0->S and G1->S progression. J. Cell Sci. 1994, 107(Pt 1):227-239.
    • (1994) J. Cell Sci. , vol.107 , Issue.PART 1 , pp. 227-239
    • Wick, M.1    Burger, C.2    Brusselbach, S.3    Lucibello, F.C.4    Muller, R.5
  • 17
    • 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. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell 2003, 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
  • 18
    • 33747877557 scopus 로고    scopus 로고
    • The Kindlins: subcellular localization and expression during murine development
    • Ussar S., Wang H.V., Linder S., Fassler R., Moser M. The Kindlins: subcellular localization and expression during murine development. Exp. Cell Res. 2006, 312:3142-3151.
    • (2006) Exp. Cell Res. , vol.312 , pp. 3142-3151
    • Ussar, S.1    Wang, H.V.2    Linder, S.3    Fassler, R.4    Moser, M.5
  • 23
    • 41949127144 scopus 로고    scopus 로고
    • Kindlin-2 Is an essential component of intercalated discs and is required for vertebrate cardiac structure and function
    • Dowling J.J., Gibbs E., Russell M., Goldman D., Minarcik J., Golden J.A., Feldman E.L. Kindlin-2 Is an essential component of intercalated discs and is required for vertebrate cardiac structure and function. Circ. Res. 2008, 102:423-431.
    • (2008) Circ. Res. , vol.102 , pp. 423-431
    • Dowling, J.J.1    Gibbs, E.2    Russell, M.3    Goldman, D.4    Minarcik, J.5    Golden, J.A.6    Feldman, E.L.7
  • 25
    • 34547120497 scopus 로고    scopus 로고
    • The MIG-2/integrin interaction strengthens cell-matrix adhesion and modulates cell motility
    • Shi X., Ma Y.Q., Tu Y., Chen K., Wu S., Fukuda K., Qin J., Plow E.F., Wu C. The MIG-2/integrin interaction strengthens cell-matrix adhesion and modulates cell motility. J. Biol. Chem. 2007, 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    Fukuda, K.6    Qin, J.7    Plow, E.F.8    Wu, C.9
  • 26
    • 43149085289 scopus 로고    scopus 로고
    • Kindlin-2 (Mig-2): a co-activator of beta3 integrins
    • Ma Y.Q., Qin J., Wu C., Plow E.F. Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J. Cell Biol. 2008, 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
  • 27
    • 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 D.S., Bouaouina M., Calderwood D.A. Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects. J. Biol. Chem. 2009, 284:11485-11497.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11485-11497
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 28
    • 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. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat. Med. 2008, 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
  • 29
    • 84863793892 scopus 로고    scopus 로고
    • Spatial coordination of kindlin-2 with talin head domain in interaction with integrin beta cytoplasmic tails
    • Bledzka K., Liu J., Xu Z., Perera H.D., Yadav S.P., Bialkowska K., Qin J., Ma Y.Q., Plow E.F. Spatial coordination of kindlin-2 with talin head domain in interaction with integrin beta cytoplasmic tails. J. Biol. Chem. 2012, 287:24585-24594.
    • (2012) J. Biol. Chem. , vol.287 , pp. 24585-24594
    • Bledzka, K.1    Liu, J.2    Xu, Z.3    Perera, H.D.4    Yadav, S.P.5    Bialkowska, K.6    Qin, J.7    Ma, Y.Q.8    Plow, E.F.9
  • 30
    • 84858779307 scopus 로고    scopus 로고
    • Kindlins integrin activation and the regulation of talin recruitment to alphaIIbbeta3
    • Kahner B.N., Kato H., Banno A., Ginsberg M.H., Shattil S.J., Ye F. Kindlins integrin activation and the regulation of talin recruitment to alphaIIbbeta3. PLoS One 2012, 7:e34056.
    • (2012) PLoS One , vol.7
    • Kahner, B.N.1    Kato, H.2    Banno, A.3    Ginsberg, M.H.4    Shattil, S.J.5    Ye, F.6
  • 31
    • 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., Wu C., Plow E.F., Ma Y.Q. Tyrosine phosphorylation of integrin beta3 regulates kindlin-2 binding and integrin activation. J. Biol. Chem. 2010, 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    Wu, C.6    Plow, E.F.7    Ma, Y.Q.8
  • 32
    • 0037451891 scopus 로고    scopus 로고
    • URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas
    • Weinstein E.J., Bourner M., Head R., Zakeri H., Bauer C., Mazzarella R. URP1: a member of a novel family of PH and FERM domain-containing membrane-associated proteins is significantly over-expressed in lung and colon carcinomas. Biochim. Biophys. Acta 2003, 1637:207-216.
    • (2003) Biochim. Biophys. Acta , vol.1637 , pp. 207-216
    • Weinstein, E.J.1    Bourner, M.2    Head, R.3    Zakeri, H.4    Bauer, C.5    Mazzarella, R.6
  • 33
    • 1342346591 scopus 로고    scopus 로고
    • The Kindler syndrome protein is regulated by transforming growth factor-beta and involved in integrin-mediated adhesion
    • Kloeker S., Major M.B., Calderwood D.A., Ginsberg M.H., Jones D.A., Beckerle M.C. The Kindler syndrome protein is regulated by transforming growth factor-beta and involved in integrin-mediated adhesion. J. Biol. Chem. 2004, 279:6824-6833.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6824-6833
    • Kloeker, S.1    Major, M.B.2    Calderwood, D.A.3    Ginsberg, M.H.4    Jones, D.A.5    Beckerle, M.C.6
  • 34
    • 83355174039 scopus 로고    scopus 로고
    • Structural basis of phosphoinositide binding to Kindlin-2 pleckstrin homology domain in regulating integrin activation
    • Liu J., Fukuda K., Xu Z., Ma Y.Q., Hirbawi J., Mao X., Wu C., Plow E.F., Qin J. Structural basis of phosphoinositide binding to Kindlin-2 pleckstrin homology domain in regulating integrin activation. J. Biol. Chem. 2011, 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    Mao, X.6    Wu, C.7    Plow, E.F.8    Qin, J.9
  • 35
    • 84863477602 scopus 로고    scopus 로고
    • Crystal structure of kindlin-2 PH domain reveals a conformational transition for its membrane anchoring and regulation of integrin activation
    • Liu Y., Zhu Y., Ye S., Zhang R. Crystal structure of kindlin-2 PH domain reveals a conformational transition for its membrane anchoring and regulation of integrin activation. Protein Cell 2012, 3:434-440.
    • (2012) Protein Cell , vol.3 , pp. 434-440
    • Liu, Y.1    Zhu, Y.2    Ye, S.3    Zhang, R.4
  • 38
    • 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 H.D., Ma Y.Q., Yang J., Hirbawi J., Plow E.F., Qin J. Membrane binding of the N-terminal ubiquitin-like domain of kindlin-2 is crucial for its regulation of integrin activation. Structure 2011, 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    Qin, J.6
  • 39
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy A., Kucukural A., Zhang Y. I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 2010, 5:725-738.
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 40
    • 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 M.A., Shattil S.J., Fukuda K., Qin J., Kretzler M., Wu C. Kindlin-2 regulates podocyte adhesion and fibronectin matrix deposition through interactions with phosphoinositides and integrins. J. Cell Sci. 2011, 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    Shattil, S.J.6    Fukuda, K.7    Qin, J.8    Kretzler, M.9    Wu, C.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.