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Volumn 110, Issue 5, 2002, Pages 587-597

A structural mechanism of integrin αIIbβ3 "inside-out" activation as regulated by its cytoplasmic face

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA2B BETA3 INTEGRIN; CYTOSKELETON PROTEIN; INTEGRIN; TALIN; UNCLASSIFIED DRUG;

EID: 0037031551     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(02)00906-6     Document Type: Article
Times cited : (458)

References (58)
  • 1
    • 0023083976 scopus 로고
    • Leukocyte adhesion deficiency: An inherited defect in the Mac-1, LFA-1, and p150,95 glycoproteins
    • Anderson D.C., Springer T.A. Leukocyte adhesion deficiency. an inherited defect in the Mac-1, LFA-1, and p150,95 glycoproteins Annu. Rev. Med. 38:1987;175-194.
    • (1987) Annu. Rev. Med. , vol.38 , pp. 175-194
    • Anderson, D.C.1    Springer, T.A.2
  • 4
  • 5
    • 84995262912 scopus 로고    scopus 로고
    • Congenital bleeding disorders with long bleeding time and normal platelet count. I. Glanzmann's thrombasthenia
    • Caen J.P., Leclerc J.C., Inceman S., Larrieu M.J., Probst M., Bernard J. Congenital bleeding disorders with long bleeding time and normal platelet count. I. Glanzmann's thrombasthenia. Am. J. Med. 41:1996;2-26.
    • (1996) Am. J. Med. , vol.41 , pp. 2-26
    • Caen, J.P.1    Leclerc, J.C.2    Inceman, S.3    Larrieu, M.J.4    Probst, M.5    Bernard, J.6
  • 6
    • 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. 274:1999;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
  • 8
    • 0027215829 scopus 로고
    • The two-dimensional transferred nuclear Overhauser effect: Theory and practice
    • Campbell A.P., Sykes B.D. The two-dimensional transferred nuclear Overhauser effect. theory and practice Annu. Rev. Biophys. Biomol. Struct. 22:1993;99-122.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 99-122
    • Campbell, A.P.1    Sykes, B.D.2
  • 9
    • 0037139592 scopus 로고    scopus 로고
    • Micelle-induced curvature in a water-insoluble HIV-1 env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel
    • Chou J.J., Kaufman J.D., Stahl J., Wingfield P.T., Bax A. Micelle-induced curvature in a water-insoluble HIV-1 env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel. J. Am. Chem. Soc. 124:2002;2450-2451.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2450-2451
    • Chou, J.J.1    Kaufman, J.D.2    Stahl, J.3    Wingfield, P.T.4    Bax, A.5
  • 10
    • 0000393431 scopus 로고
    • The two-dimensional transferred nuclear Overhauser effect
    • Clore G.M., Gronenborn A.M. The two-dimensional transferred nuclear Overhauser effect. J. Magn. Reson. 48:1982;402-417.
    • (1982) J. Magn. Reson. , vol.48 , pp. 402-417
    • Clore, G.M.1    Gronenborn, A.M.2
  • 11
    • 0031933143 scopus 로고    scopus 로고
    • Determining the structures of large proteins and protein complexes by NMR
    • Clore G.M., Gronenborn A.M. Determining the structures of large proteins and protein complexes by NMR. Trends Biotechnol. 16:1998;22-34.
    • (1998) Trends Biotechnol. , vol.16 , pp. 22-34
    • Clore, G.M.1    Gronenborn, A.M.2
  • 14
    • 0030898798 scopus 로고    scopus 로고
    • A conserved sequence motif in the integrin beta3 cytoplasmic domain is required for its specific interaction with beta3-endonexin
    • Eigenthaler M., Hofferer L., Shattil S.J., Ginsberg M.H. A conserved sequence motif in the integrin beta3 cytoplasmic domain is required for its specific interaction with beta3-endonexin. J. Biol. Chem. 272:1997;7693-7698.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7693-7698
    • Eigenthaler, M.1    Hofferer, L.2    Shattil, S.J.3    Ginsberg, M.H.4
  • 15
    • 0033794003 scopus 로고    scopus 로고
    • NMR spectroscopy: A multifaceted approach to macromolecular structure
    • Ferentz A.E., Wagner G. NMR spectroscopy. a multifaceted approach to macromolecular structure Q. Rev. Biophys. 33:2000;29-65.
    • (2000) Q. Rev. Biophys. , vol.33 , pp. 29-65
    • Ferentz, A.E.1    Wagner, G.2
  • 16
    • 0022369034 scopus 로고
    • A method for purifying the platelet membrane glycoprotein IIb-IIIa complex
    • Fitzgerald L.A., Leung B., Phillips D.R. A method for purifying the platelet membrane glycoprotein IIb-IIIa complex. Anal. Biochem. 151:1985;169-177.
    • (1985) Anal. Biochem. , vol.151 , pp. 169-177
    • Fitzgerald, L.A.1    Leung, B.2    Phillips, D.R.3
  • 17
    • 0026537207 scopus 로고
    • Role of the transmembrane and cytoplasmic domains in the assembly and surface exposure of the platelet integrin GPIIb/IIIa
    • Frachet P., Duperray A., Delachanal E., Marguerie G. Role of the transmembrane and cytoplasmic domains in the assembly and surface exposure of the platelet integrin GPIIb/IIIa. Biochemistry. 31:1992;2408-2415.
    • (1992) Biochemistry , vol.31 , pp. 2408-2415
    • Frachet, P.1    Duperray, A.2    Delachanal, E.3    Marguerie, G.4
  • 18
    • 0000041361 scopus 로고
    • A common sense approach to peak picking in two- three- and four-dimensional spectra using automatic computer analysis of contour diagrams
    • Garrett D.S., Powers R., Gronenborn A.M., Clore G.M. A common sense approach to peak picking in two- three- and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95:1991;214-220.
    • (1991) J. Magn. Reson. , vol.95 , pp. 214-220
    • Garrett, D.S.1    Powers, R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 19
  • 21
    • 0029665001 scopus 로고    scopus 로고
    • 3: A ternary complex of the integrin α and β subunits and a divalent cation
    • 3. a ternary complex of the integrin α and β subunits and a divalent cation J. Biol. Chem. 271:1996;6017-6026.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6017-6026
    • Haas, T.A.1    Plow, E.F.2
  • 22
    • 0031404511 scopus 로고    scopus 로고
    • Development of a structural model for the cytoplasmic domain of an integrin
    • Haas T.A., Plow E.F. Development of a structural model for the cytoplasmic domain of an integrin. Protein Eng. 10:1997;1395-1405.
    • (1997) Protein Eng. , vol.10 , pp. 1395-1405
    • Haas, T.A.1    Plow, E.F.2
  • 23
    • 0032168738 scopus 로고    scopus 로고
    • Integrin affinity modulation
    • Hughes P.E., Pfaff M. Integrin affinity modulation. Trends Cell Biol. 8:1998;359-364.
    • (1998) Trends Cell Biol. , vol.8 , pp. 359-364
    • Hughes, P.E.1    Pfaff, M.2
  • 24
    • 0029048813 scopus 로고
    • The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity
    • Hughes P.E., O'Toole T.E., Ylanne J., Shattil S.J., Ginsberg M.H. The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity. J. Biol. Chem. 270:1995;12411-12417.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12411-12417
    • Hughes, P.E.1    O'Toole, T.E.2    Ylanne, J.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 26
    • 0023666065 scopus 로고
    • Integrins: A family of cell surface receptors
    • Hynes R.O. Integrins. a family of cell surface receptors Cell. 48:1987;549-550.
    • (1987) Cell , vol.48 , pp. 549-550
    • Hynes, R.O.1
  • 27
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes R.O. Integrins. versatility, modulation, and signaling in cell adhesion Cell. 69:1992;11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 28
    • 0000165109 scopus 로고
    • Isotope-filtered 2D NMR of a protein-peptide complex: Study of a skeletal muscle myosin light chain kinase fragment bound to calmodulin
    • Ikura M., Bax A. Isotope-filtered 2D NMR of a protein-peptide complex. study of a skeletal muscle myosin light chain kinase fragment bound to calmodulin J. Am. Chem. Soc. 114:1992;2433-2440.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 2433-2440
    • Ikura, M.1    Bax, A.2
  • 29
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust R.B., Waugh D.S. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8:1999;1668-1674.
    • (1999) Protein Sci. , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 31
    • 0029881007 scopus 로고    scopus 로고
    • Molmol: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wuthrich K. Molmol. a program for display and analysis of macromolecular structures J. Mol. Graph. 14:1996;51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 33
    • 0035940359 scopus 로고    scopus 로고
    • Oligomerization of the integrin alphaIIbbeta3: Roles of the transmembrane and cytoplasmic domains
    • Li R., Babu C.R., Lear J.D., Wand A.J., Bennett J.S., DeGrado W.F. Oligomerization of the integrin alphaIIbbeta3. roles of the transmembrane and cytoplasmic domains Proc. Natl. Acad. Sci. USA. 98:2001;12462-12467.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12462-12467
    • Li, R.1    Babu, C.R.2    Lear, J.D.3    Wand, A.J.4    Bennett, J.S.5    DeGrado, W.F.6
  • 34
    • 0035805633 scopus 로고    scopus 로고
    • Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state
    • Lu C., Takagi J., Springer T.A. Association of the membrane proximal regions of the alpha and beta subunit cytoplasmic domains constrains an integrin in the inactive state. J. Biol. Chem. 276:2001;14642-14648.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14642-14648
    • Lu, C.1    Takagi, J.2    Springer, T.A.3
  • 38
    • 0033214440 scopus 로고    scopus 로고
    • Identification of a talin-binding site in the integrin beta(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin N-terminal head domain interacts with the membrane-proximal region of the beta(3) cytoplasmic tail
    • Patil S., Jedsadayanmata A., Wencel-Drake J.D., Wang W., Knezevic I., Lam S.C. Identification of a talin-binding site in the integrin beta(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin N-terminal head domain interacts with the membrane-proximal region of the beta(3) cytoplasmic tail. J. Biol. Chem. 274:1999;28575-28583.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28575-28583
    • Patil, S.1    Jedsadayanmata, A.2    Wencel-Drake, J.D.3    Wang, W.4    Knezevic, I.5    Lam, S.C.6
  • 39
    • 0032530888 scopus 로고    scopus 로고
    • 3 (GPIIb-IIIa) assumes an active, ligand-binding conformation and is recognized by GPIIb-IIIa specific monoclonal, allo-, auto-, and drug-dependent platelet antibodies
    • 3 (GPIIb-IIIa) assumes an active, ligand-binding conformation and is recognized by GPIIb-IIIa specific monoclonal, allo-, auto-, and drug-dependent platelet antibodies. Blood. 92:1998;2053-2063.
    • (1998) Blood , vol.92 , pp. 2053-2063
    • Peterson, J.A.1    Visentin, G.P.2    Newman, P.J.3    Aster, R.H.4
  • 40
    • 0032513019 scopus 로고    scopus 로고
    • Integrin beta cytoplasmic domains differentially bind to cytoskeletal proteins
    • Pfaff M., Liu S., Erle D.J., Ginsberg M.H. Integrin beta cytoplasmic domains differentially bind to cytoskeletal proteins. J. Biol. Chem. 273:1998;6104-6109.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6104-6109
    • Pfaff, M.1    Liu, S.2    Erle, D.J.3    Ginsberg, M.H.4
  • 41
    • 0032762593 scopus 로고    scopus 로고
    • The biology of glycoprotein IIb-IIIa
    • Plow E.F., Byzova T. The biology of glycoprotein IIb-IIIa. Coron. Artery Dis. 10:1999;547-551.
    • (1999) Coron. Artery Dis. , vol.10 , pp. 547-551
    • Plow, E.F.1    Byzova, T.2
  • 43
  • 45
    • 0031471678 scopus 로고    scopus 로고
    • Perspective series: Cell adhesion in vascular biology. Integrin signaling in vascular biology
    • Shattil S.J., Ginsberg M.H. Perspective series. cell adhesion in vascular biology. Integrin signaling in vascular biology J. Clin. Invest. 100:1997;S91-S95.
    • (1997) J. Clin. Invest. , vol.100
    • Shattil, S.J.1    Ginsberg, M.H.2
  • 46
    • 0347610773 scopus 로고
    • β chemical shifts to the protein secondary structure
    • β chemical shifts to the protein secondary structure. J. Am. Chem. Soc. 113:1991;5490-5492.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 47
    • 0035041854 scopus 로고    scopus 로고
    • C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1
    • Takagi J., Erickson H.P., Springer T.A. C-terminal opening mimics 'inside-out' activation of integrin alpha5beta1. Nat. Struct. Biol. 8:2001;412-416.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 412-416
    • Takagi, J.1    Erickson, H.P.2    Springer, T.A.3
  • 48
    • 0037127264 scopus 로고    scopus 로고
    • Calcium integrin-binding protein activates platelet integrin alphaIIb beta3
    • Tsuboi S. Calcium integrin-binding protein activates platelet integrin alphaIIb beta3. J. Biol. Chem. 277:2002;1919-1923.
    • (2002) J. Biol. Chem. , vol.277 , pp. 1919-1923
    • Tsuboi, S.1
  • 49
    • 0035954396 scopus 로고    scopus 로고
    • NMR analysis of structure and dynamics of the cytosolic tails of integrin alphaIIb beta3 in aqueous solution
    • Ulmer T.S., Yaspan B., Ginsberg M.H., Campbell I.D. NMR analysis of structure and dynamics of the cytosolic tails of integrin alphaIIb beta3 in aqueous solution. Biochemistry. 40:2001;7498-7508.
    • (2001) Biochemistry , vol.40 , pp. 7498-7508
    • Ulmer, T.S.1    Yaspan, B.2    Ginsberg, M.H.3    Campbell, I.D.4
  • 52
    • 0037197990 scopus 로고    scopus 로고
    • Solution structures of the cytoplasmic tail complex from platelet integrin alpha IIb- and beta 3-subunits
    • Weljie A.M., Hwang P.M., Vogel H.J. Solution structures of the cytoplasmic tail complex from platelet integrin alpha IIb- and beta 3-subunits. Proc. Natl. Acad. Sci. USA. 99:2002;5878-5883.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5878-5883
    • Weljie, A.M.1    Hwang, P.M.2    Vogel, H.J.3
  • 55
    • 0035958967 scopus 로고    scopus 로고
    • Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain
    • Yan B., Calderwood D.A., Yaspan B., Ginsberg M.H. Calpain cleavage promotes talin binding to the beta 3 integrin cytoplasmic domain. J. Biol. Chem. 276:2001;28164-28170.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28164-28170
    • Yan, B.1    Calderwood, D.A.2    Yaspan, B.3    Ginsberg, M.H.4
  • 57
    • 0034987544 scopus 로고    scopus 로고
    • A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins
    • Zhou P., Lugovskoy A.A., Wagner G. A solubility-enhancement tag (SET) for NMR studies of poorly behaving proteins. J. Biomol. NMR. 20:2001;11-14.
    • (2001) J. Biomol. NMR , vol.20 , pp. 11-14
    • Zhou, P.1    Lugovskoy, A.A.2    Wagner, G.3
  • 58
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy: Application to a bacteriophage λ N-peptide/boxB RNA complex
    • Zwahlen C., Legault P., Vincent S.J.F., Greenblatt J., Konrat R., Kay L.E. Methods for measurement of intermolecular NOEs by multinuclear NMR spectroscopy. application to a bacteriophage λ N-peptide/boxB RNA complex J. Am. Chem. Soc. 119:1997;711-721.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 711-721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.J.F.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6


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