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Volumn 287, Issue 45, 2012, Pages 37715-37731

Biophysical analysis of kindlin-3 reveals an elongated conformation and maps integrin binding to the membrane-distal β-subunit NPXY motif

Author keywords

[No Author keywords available]

Indexed keywords

BIOPHYSICAL ANALYSIS; COACTIVATORS; ELONGATED STRUCTURES; INTEGRIN BINDING; INTEGRINS; SOLUTION STRUCTURES; TERNARY COMPLEX;

EID: 84868306936     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.415208     Document Type: Article
Times cited : (32)

References (58)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-6877
    • (2002) Cell , vol.110 , pp. 673-6877
    • Hynes, R.O.1
  • 4
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, Talin, and Kindlins
    • Moser, M., Legate, K. R., Zent, R., and Fässler, R. (2009) The tail of integrins, Talin, and Kindlins. Science 324, 895-8999
    • (2009) Science , vol.324 , pp. 895-8999
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fässler, R.4
  • 6
    • 70349312643 scopus 로고    scopus 로고
    • The Kindlin protein family: New members to the club of focal adhesion proteins
    • Meves, A., Stremmel, C., Gottschalk, K., and Fässler, R. (2009) The Kindlin protein family: new members to the club of focal adhesion proteins. Trends Cell Biol. 19, 504-5133
    • (2009) Trends Cell Biol. , vol.19 , pp. 504-5133
    • Meves, A.1    Stremmel, C.2    Gottschalk, K.3    Fässler, R.4
  • 9
    • 33747877557 scopus 로고    scopus 로고
    • The Kindlins: Subcellular localization and expression during murine development
    • Ussar, S., Wang, H. V., Linder, S., Fässler, R., and Moser, M. (2006) The Kindlins: subcellular localization and expression during murine development. Exp. Cell Res. 312, 3142-31511
    • (2006) Exp. Cell Res. , vol.312 , pp. 3142-31511
    • Ussar, S.1    Wang, H.V.2    Linder, S.3    Fässler, R.4    Moser, M.5
  • 13
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • Moser, M., Nieswandt, B., Ussar, S., Pozgajova, M., and Fässler, R. (2008) Kindlin-3 is essential for integrin activation and platelet aggregation. Nat. Med. 14, 325-3300
    • (2008) Nat. Med. , vol.14 , pp. 325-3300
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fässler, R.5
  • 17
    • 78649781976 scopus 로고    scopus 로고
    • Structural diversity in integrin/Talin interactions
    • Anthis, N. J., Wegener, K. L., Critchley, D. R., and Campbell, I. D. (2010) Structural diversity in integrin/Talin interactions. Structure 18, 1654-16666
    • (2010) Structure , vol.18 , pp. 1654-16666
    • Anthis, N.J.1    Wegener, K.L.2    Critchley, D.R.3    Campbell, I.D.4
  • 19
    • 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, D. S., Bouaouina, M., and Calderwood, D. A. (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, 11485-114977
    • (2009) J. Biol. Chem. , vol.284 , pp. 11485-114977
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 21
    • 1342346591 scopus 로고    scopus 로고
    • The Kindler syndrome protein is regulated by transforming growth factor-β and involved in integrin-mediated adhesion
    • Kloeker, S., Major, M. B., Calderwood, D. A., Ginsberg, M. H., Jones, D. A., and Beckerle, M. C. (2004) The Kindler syndrome protein is regulated by transforming growth factor-β and involved in integrin-mediated adhesion. J. Biol. Chem. 279, 6824-68333
    • (2004) J. Biol. Chem. , vol.279 , pp. 6824-68333
    • Kloeker, S.1    Major, M.B.2    Calderwood, D.A.3    Ginsberg, M.H.4    Jones, D.A.5    Beckerle, M.C.6
  • 22
    • 43149085289 scopus 로고    scopus 로고
    • Kindlin-2 (Mig-2): A co-activator of β3 integrins
    • Ma, Y. Q., Qin, J., Wu, C., and Plow, E. F. (2008) Kindlin-2 (Mig-2): a co-activator of β3 integrins. J. Cell Biol. 181, 439-4466
    • (2008) J. Cell Biol. , vol.181 , pp. 439-4466
    • Ma, Y.Q.1    Qin, J.2    Wu, C.3    Plow, E.F.4
  • 24
    • 84863793892 scopus 로고    scopus 로고
    • Spatial coordination of Kindlin-2 with Talin head domain in interaction with integrin β cytoplasmic tails
    • Bledzka, K., Liu, J., Xu, Z., Perera, H. D., Yadav, S. P., Bialkowska, K., Qin, J., Ma, Y. Q., and Plow, E. F. (2012) Spatial coordination of Kindlin-2 with Talin head domain in interaction with integrin β cytoplasmic tails. J. Biol. Chem. 287, 24585-245944
    • (2012) J. Biol. Chem. , vol.287 , pp. 24585-245944
    • 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
  • 26
    • 84866168074 scopus 로고    scopus 로고
    • Distinct roles of Talin and Kindlin in regulating integrin α5β1 function and trafficking
    • Margadant, C., Kreft, M., de Groot, D. J., Norman, J. C., and Sonnenberg, A. (2012) Distinct roles of Talin and Kindlin in regulating integrin α5β1 function and trafficking. Curr. Biol. 22, 1554-15633
    • (2012) Curr. Biol. , vol.22 , pp. 1554-15633
    • Margadant, C.1    Kreft, M.2    De Groot, D.J.3    Norman, J.C.4    Sonnenberg, A.5
  • 29
    • 41949131361 scopus 로고    scopus 로고
    • An integrin phosphorylation switch: The effect of 3 integrin tail phosphorylation on Dok1 and Talin binding
    • Oxley, C. L., Anthis, N. J., Lowe, E. D., Vakonakis, I., Campbell, I. D., and Wegener, K. L. (2008) An integrin phosphorylation switch: the effect of 3 integrin tail phosphorylation on Dok1 and Talin binding. J. Biol. Chem. 283, 5420-54266
    • (2008) J. Biol. Chem. , vol.283 , pp. 5420-54266
    • Oxley, C.L.1    Anthis, N.J.2    Lowe, E.D.3    Vakonakis, I.4    Campbell, I.D.5    Wegener, K.L.6
  • 30
    • 33744809773 scopus 로고    scopus 로고
    • Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation
    • Brown, P. H., and Schuck, P. (2006) Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation. Biophys. J. 90, 4651-46611
    • (2006) Biophys. J. , vol.90 , pp. 4651-46611
    • Brown, P.H.1    Schuck, P.2
  • 33
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun, D. I. (1992) Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25, 495-5033
    • (1992) J. Appl. Crystallogr. , vol.25 , pp. 495-5033
    • Svergun, D.I.1
  • 34
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • Svergun, D. I., Petoukhov, M. V., and Koch, M. H. (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys. J. 80, 2946-29533
    • (2001) Biophys. J. , vol.80 , pp. 2946-29533
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.3
  • 35
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov, V. V., and Svergun, D. I. (2003) Uniqueness of ab initio shape determination in small-angle scattering. J. Appl. Crystallogr. 36, 860-8644
    • (2003) J. Appl. Crystallogr. , vol.36 , pp. 860-8644
    • Volkov, V.V.1    Svergun, D.I.2
  • 38
    • 0033777020 scopus 로고    scopus 로고
    • Resolution measurement in structures derived from single particles
    • Grigorieff, N. (2000) Resolution measurement in structures derived from single particles. Acta Crystallogr. D Biol. Crystallogr. 56, 1270-12777
    • (2000) Acta Crystallogr. D Biol. Crystallogr. , vol.56 , pp. 1270-12777
    • Grigorieff, N.1
  • 39
    • 33847065474 scopus 로고    scopus 로고
    • Improved calculation of rotational diffusion and intrinsic viscosity of bead models for macromolecules and nanoparticles
    • de la Torre, J. G., Echenique Gdel, R., and Ortega, A. (2007) Improved calculation of rotational diffusion and intrinsic viscosity of bead models for macromolecules and nanoparticles. J. Phys. Chem. B 111, 955-9611
    • (2007) J. Phys. Chem. B , vol.111 , pp. 955-9611
    • De La Torre, J.G.1    Echenique Gdel, R.2    Ortega, A.3
  • 40
    • 0006159290 scopus 로고
    • Einige Neuerungen in der Technik und Auswertung von Röntgen- Kleinwinkelmessungen
    • Kratky, O., Porod, G., and Kahovec, L. (1951) Einige Neuerungen in der Technik und Auswertung von Röntgen-Kleinwinkelmessungen. Z. Elektrochem. 55, 53-599
    • (1951) Z. Elektrochem. , vol.55 , pp. 53-599
    • Kratky, O.1    Porod, G.2    Kahovec, L.3
  • 41
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov, M. V., and Svergun, D. I. (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys. J. 89, 1237-12500
    • (2005) Biophys. J. , vol.89 , pp. 1237-12500
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 42
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-2933
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-2933
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 43
    • 0004040543 scopus 로고    scopus 로고
    • University of California, San Franciscoo
    • Goddard, T. D., and Kneller, D. G. (2000) SPARKY 3, University of California, San Franciscoo
    • (2000) SPARKY 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 46
    • 84858779307 scopus 로고    scopus 로고
    • Kindlins, integrin activation, and the regulation of Talin recruitment to αiIbβ3
    • Kahner, B. N., Kato, H., Banno, A., Ginsberg, M. H., Shattil, S. J., and Ye, F. (2012) Kindlins, integrin activation, and the regulation of Talin recruitment to αIIbβ3. PLoS One 7, e340566
    • (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
  • 49
    • 0031453963 scopus 로고    scopus 로고
    • OLDERADO: On-line database of ensemble representatives and domains
    • Kelley, L. A., and Sutcliffe, M. J. (1997) OLDERADO: on-line database of ensemble representatives and domains. Protein Sci. 6, 2628-26300
    • (1997) Protein Sci. , vol.6 , pp. 2628-26300
    • Kelley, L.A.1    Sutcliffe, M.J.2
  • 50
    • 84865257028 scopus 로고    scopus 로고
    • AMolecular mechanism for the requirement of PAT-4 (integrin-linked kinase (ILK)) for the localization of UNC-112 (Kindlin) to integrin adhesion sites
    • Qadota, H., Moerman, D. G., and Benian, G. M. (2012)AMolecular mechanism for the requirement of PAT-4 (integrin-linked kinase (ILK)) for the localization of UNC-112 (Kindlin) to integrin adhesion sites. J. Biol. Chem. 287, 28537-285511
    • (2012) J. Biol. Chem. , vol.287 , pp. 28537-285511
    • Qadota, H.1    Moerman, D.G.2    Benian, G.M.3
  • 52
    • 61449213806 scopus 로고    scopus 로고
    • Mechanisms that regulate adaptor binding to β-integrin cytoplasmic tails
    • Legate, K. R., and Fässler, R. (2009) Mechanisms that regulate adaptor binding to β-integrin cytoplasmic tails. J. Cell Sci. 122, 187-1988
    • (2009) J. Cell Sci. , vol.122 , pp. 187-1988
    • Legate, K.R.1    Fässler, R.2
  • 53
    • 77957269801 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of integrin β3 regulates Kindlin-2 binding and integrin activation
    • Bledzka, K., Bialkowska, K., Nie, H., Qin, J., Byzova, T., Wu, C., Plow, E. F., and Ma, Y. Q. (2010) Tyrosine phosphorylation of integrin β3 regulates Kindlin-2 binding and integrin activation. J. Biol. Chem. 285, 30370-303744
    • (2010) J. Biol. Chem. , vol.285 , pp. 30370-303744
    • 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
  • 54
  • 55
    • 0033592610 scopus 로고    scopus 로고
    • Integrin cytoplasmic tyrosine motif is required for outside-in αiIbβ3 signalling and platelet function
    • Law, D. A., DeGuzman, F. R., Heiser, P., Ministri-Madrid, K., Killeen, N., and Phillips, D. R. (1999) Integrin cytoplasmic tyrosine motif is required for outside-in αIIbβ3 signalling and platelet function. Nature 401, 808-8111
    • (1999) Nature , vol.401 , pp. 808-8111
    • Law, D.A.1    Deguzman, F.R.2    Heiser, P.3    Ministri-Madrid, K.4    Killeen, N.5    Phillips, D.R.6
  • 56
    • 84861622962 scopus 로고    scopus 로고
    • Sorting Nexin 17 prevents lysosomal degradation of β1 integrins by binding to the β1-integrin tail
    • Böttcher, R. T., Stremmel, C., Meves, A., Meyer, H., Widmaier, M., Tseng, H. Y., and Fässler, R. (2012) Sorting Nexin 17 prevents lysosomal degradation of β1 integrins by binding to the β1-integrin tail. Nat. Cell Biol. 14, 584-5922
    • (2012) Nat. Cell Biol. , vol.14 , pp. 584-5922
    • Böttcher, R.T.1    Stremmel, C.2    Meves, A.3    Meyer, H.4    Widmaier, M.5    Tseng, H.Y.6    Fässler, R.7
  • 57
    • 0032961270 scopus 로고    scopus 로고
    • ESPript: Analysis of multiple sequence alignments in PostScript
    • Gouet, P., Courcelle, E., Stuart, D. I., and Métoz, F. (1999) ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 15, 305-3088
    • (1999) Bioinformatics , vol.15 , pp. 305-3088
    • Gouet, P.1    Courcelle, E.2    Stuart, D.I.3    Métoz, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.