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Volumn 3, Issue 6, 2012, Pages 434-440

Crystal structure of kindlin-2 PH domain reveals a conformational transition for its membrane anchoring and regulation of integrin activation

Author keywords

cell adhesion; crystal structure; integrin; kindlin 2; membrane; PH domain

Indexed keywords

FERM DOMAIN CONTAING PROTEIN; INTEGRIN; KINDLIN 2 PROTEIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PROTEIN; UNCLASSIFIED DRUG;

EID: 84863477602     PISSN: 1674800X     EISSN: 16748018     Source Type: Journal    
DOI: 10.1007/s13238-012-2046-1     Document Type: Article
Times cited : (27)

References (27)
  • 3
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley, P., and Cowtan, K. (2004). Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60, 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 5
    • 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., and Calderwood, D. A. (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
  • 6
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes, R. O. (2002). Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 7
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim, M., Carman, C. V., and Springer, T. A. (2003). Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 301, 1720-1725.
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 8
    • 79958111313 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray crystallographic analysis of the human kindlin-2 PH domain
    • Lee, J. H., An, J. Y., Park, H., Kim, H. J., and Eom, S. H. (2011). Crystallization and preliminary x-ray crystallographic analysis of the human kindlin-2 PH domain. Acta Crystallogr Sect F Struct Biol Cryst Commun 67, 696-699.
    • (2011) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.67 , pp. 696-699
    • Lee, J.H.1    An, J.Y.2    Park, H.3    Kim, H.J.4    Eom, S.H.5
  • 9
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M. A. (2008). Membrane recognition by phospholipid-binding domains. Nat Rev Mol Cell Biol 9, 99-111.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 10
    • 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, Y. Q., Hirbawi, J., Mao, X., Wu, C., Plow, E. F., and Qin, J. (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    Mao, X.6    Wu, C.7    Plow, E.F.8    Qin, J.9
  • 11
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo, B. H., Carman, C. V., and Springer, T. A. (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
  • 12
    • 43149085289 scopus 로고    scopus 로고
    • Kindlin-2 (Mig-2): a co-activator of beta3 integrins
    • Ma, Y. Q., Qin, J., Wu, C., and Plow, E. F. (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
  • 14
    • 0242468741 scopus 로고    scopus 로고
    • Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change
    • Milburn, C. C., Deak, M., Kelly, S. M., Price, N. C., Alessi, D. R., and van Aalten, D. M. (2003). Binding of phosphatidylinositol 3, 4, 5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change. Biochem J 375, 531-538.
    • (2003) Biochem J , vol.375 , pp. 531-538
    • Milburn, C.C.1    Deak, M.2    Kelly, S.M.3    Price, N.C.4    Alessi, D.R.5    van Aalten, D.M.6
  • 16
    • 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, 895-899.
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fässler, R.4
  • 17
    • 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, 325-330.
    • (2008) Nat Med , vol.14 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fässler, R.5
  • 18
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol 276, 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 19
    • 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., and Qin, J. (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    Qin, J.6
  • 20
    • 69549114537 scopus 로고    scopus 로고
    • Kindling the flame of integrin activation and function with kindlins
    • Plow, E. F., Qin, J., and Byzova, T. (2009). Kindling the flame of integrin activation and function with kindlins. Curr Opin Hematol 16, 323-328.
    • (2009) Curr Opin Hematol , vol.16 , pp. 323-328
    • Plow, E.F.1    Qin, J.2    Byzova, T.3
  • 21
    • 16644368209 scopus 로고    scopus 로고
    • Integrin bidirectional signaling: a molecular view
    • Qin, J., Vinogradova, O., and Plow, E. F. (2004). Integrin bidirectional signaling: a molecular view. PLoS Biol 2, e169.
    • (2004) PLoS Biol , vol.2
    • Qin, J.1    Vinogradova, O.2    Plow, E.F.3
  • 22
    • 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., and Wu, C. (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    Shattil, S.J.6    Fukuda, K.7    Qin, J.8    Kretzler, M.9    Wu, C.10
  • 23
    • 0034632070 scopus 로고    scopus 로고
    • The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane
    • Rogalski, T. M., Mullen, G. P., Gilbert, M. M., Williams, B. D., and Moerman, D. G. (2000). The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane. J Cell Biol 150, 253-264.
    • (2000) J Cell Biol , vol.150 , pp. 253-264
    • Rogalski, T.M.1    Mullen, G.P.2    Gilbert, M.M.3    Williams, B.D.4    Moerman, D.G.5
  • 24
    • 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., and Wu, C. (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    Fukuda, K.6    Qin, J.7    Plow, E.F.8    Wu, C.9
  • 26
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin alpha(IIb)beta(3) "inside-out" activation as regulated by its cytoplasmic face
    • Vinogradova, O., Velyvis, A., Velyviene, A., Hu, B., Haas, T., Plow, E., and Qin, J. (2002). A structural mechanism of integrin alpha(IIb)beta(3) "inside-out" activation as regulated by its cytoplasmic face. Cell 110, 587-597.
    • (2002) Cell , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.5    Plow, E.6    Qin, J.7
  • 27
    • 84863258188 scopus 로고    scopus 로고
    • Integrin signalling and function in immune cells
    • Zhang, Y., and Wang, H. (2012). Integrin signalling and function in immune cells. Immunology 135, 268-275.
    • (2012) Immunology , vol.135 , pp. 268-275
    • Zhang, Y.1    Wang, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.