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Volumn 15, Issue 1, 2004, Pages 43-54

Calreticulin-independent regulation of the platelet integrin α IIbβ3 by the KVGFFKR αIIb- cytoplasmic motif

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; BINDING PROTEIN; CALRETICULIN; DIVALENT CATION; FIBRINOGEN RECEPTOR; LYSYLVALYLGLYCYLPHENYLALANYLPHENYLALANYLLYSYLARGININE; PEPTIDE; PROTEIN SUBUNIT; TALIN; UNCLASSIFIED DRUG;

EID: 1442277113     PISSN: 09537104     EISSN: None     Source Type: Journal    
DOI: 10.1080/09537100310001640055     Document Type: Article
Times cited : (8)

References (40)
  • 1
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes R. Integrins: bidirectional, allosteric signaling machines. Cell 2002; 110: 673-87.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.1
  • 2
    • 0032523064 scopus 로고    scopus 로고
    • Integrin signaling: The platelet paradigm
    • Shattil S J, Kashiwagi H, Pampori N. Integrin signaling: the platelet paradigm. Blood 1998; 91: 2645-57.
    • (1998) Blood , vol.91 , pp. 2645-2657
    • Shattil, S.J.1    Kashiwagi, H.2    Pampori, N.3
  • 3
    • 0033731119 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-binding proteins
    • Liu S, Calderwood D A, Ginsberg M H. Integrin cytoplasmic domain-binding proteins. J Cell Sci 2000; 113(Pt 20): 3563-71.
    • (2000) J Cell Sci , vol.113 , Issue.20 PART , pp. 3563-3571
    • Liu, S.1    Calderwood, D.A.2    Ginsberg, M.H.3
  • 4
    • 0032493816 scopus 로고    scopus 로고
    • A sequence within the cytoplasmic tail of GpIIb independently activates platelet aggregation and thromboxane synthesis
    • Stephens G, O'Luanaigh N, Reilly D, Harriott P, Walker B, Fitzgerald D, Moran N. A sequence within the cytoplasmic tail of GpIIb independently activates platelet aggregation and thromboxane synthesis. J Biol Chem 1998; 273: 20317-22.
    • (1998) J Biol Chem , vol.273 , pp. 20317-20322
    • Stephens, G.1    O'Luanaigh, N.2    Reilly, D.3    Harriott, P.4    Walker, B.5    Fitzgerald, D.6    Moran, N.7
  • 5
    • 0031046185 scopus 로고    scopus 로고
    • Identification of a novel calcium-binding protein that interacts with the integrin αIIb cytoplasmic domain
    • Naik U P, Patel P M, Parise L V. Identification of a novel calcium-binding protein that interacts with the integrin αIIb cytoplasmic domain. J Biol Chem 1997; 272: 4651-4.
    • (1997) J Biol Chem , vol.272 , pp. 4651-4654
    • Naik, U.P.1    Patel, P.M.2    Parise, L.V.3
  • 6
    • 0033568191 scopus 로고    scopus 로고
    • Calcium-dependent properties of CIB binding to the integrin αIIb cytoplasmic domain and translocation to the platelet cytoskeleton
    • Shock D D, Naik U P, Brittain J E, Alahari S K, Sondek J, Parise L V. Calcium-dependent properties of CIB binding to the integrin αIIb cytoplasmic domain and translocation to the platelet cytoskeleton. Biochem J 1999; 342: 729-35.
    • (1999) Biochem J , vol.342 , pp. 729-735
    • Shock, D.D.1    Naik, U.P.2    Brittain, J.E.3    Alahari, S.K.4    Sondek, J.5    Parise, L.V.6
  • 8
    • 0029945019 scopus 로고    scopus 로고
    • A deletion in the alpha subunit locks platelet integrin αIIbβ3 into a high affinity state
    • Peter K, Bode C. A deletion in the alpha subunit locks platelet integrin αIIbβ3 into a high affinity state. Blood Coagul Fibrinolysis 1996; 2: 233-6.
    • (1996) Blood Coagul Fibrinolysis , vol.2 , pp. 233-236
    • Peter, K.1    Bode, C.2
  • 10
    • 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 1995; 270: 12411-7.
    • (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
  • 12
    • 0035940359 scopus 로고    scopus 로고
    • Oligomerization of the integrin αIIbβ3: Roles of the transmembrane and cytoplasmic domains
    • Li R, Babu C R, Lear J D, Wand A J, Bennett J S, de Grado W F. Oligomerization of the integrin αIIbβ3: roles of the transmembrane and cytoplasmic domains. Proc Natl Acad Sci USA 2001; 98: 12462-7.
    • (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    De Grado, W.F.6
  • 13
    • 0035954396 scopus 로고    scopus 로고
    • NMR analysis of structure and dynamics of the cytosolic tails of integrin αIIbβ3 in aqueous solution
    • Ulmer T S, Yaspan B, Ginsberg M H, Campbell ID. NMR analysis of structure and dynamics of the cytosolic tails of integrin αIIbβ3 in aqueous solution. Biochemistry 2001; 40: 7498-508.
    • (2001) Biochemistry , vol.40 , pp. 7498-7508
    • Ulmer, T.S.1    Yaspan, B.2    Ginsberg, M.H.3    Campbell, I.D.4
  • 14
    • 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 HJ. Solution structures of the cytoplasmic tail complex from platelet integrin alpha IIb- and beta 3-subunits. Proc Natl Acad Sci USA 2002; 99: 5878-83.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5878-5883
    • Weljie, A.M.1    Hwang, P.M.2    Vogel, H.J.3
  • 15
    • 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, Plow E, Qin J. A structural mechanism of integrin αIIbβ3 'inside-out' activation as regulated by its cytoplasmic face. Cell 2002; 110: 587.
    • (2002) Cell , vol.110 , pp. 587
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.5    Plow, E.6    Qin, J.7
  • 16
    • 0026069822 scopus 로고
    • In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin α subunits
    • Rojiani M V, Finlay B B, Gray V, Dedhar S. In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin α subunits. Biochemistry 1991; 30: 9859-66.
    • (1991) Biochemistry , vol.30 , pp. 9859-9866
    • Rojiani, M.V.1    Finlay, B.B.2    Gray, V.3    Dedhar, S.4
  • 17
    • 0037047274 scopus 로고    scopus 로고
    • Ancient ubiquitous protein 1 binds to the conserved membrane-proximal sequence of the cytoplasmic tail of the integrin α subunits that plays a crucial role in the inside-out signaling of αIIbβ3
    • Kato A, Kawamata N, Tamayose K, Egashira M, Miura R, Fujimura T, Murayama K, Oshimi K. Ancient ubiquitous protein 1 binds to the conserved membrane-proximal sequence of the cytoplasmic tail of the integrin α subunits that plays a crucial role in the inside-out signaling of αIIbβ3. J Biol Chem 2002; 277: 28934-41.
    • (2002) J Biol Chem , vol.277 , pp. 28934-28941
    • Kato, A.1    Kawamata, N.2    Tamayose, K.3    Egashira, M.4    Miura, R.5    Fujimura, T.6    Murayama, K.7    Oshimi, K.8
  • 18
    • 0028323266 scopus 로고
    • Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin alpha-subunit-binding protein
    • Leung-Hagesteijn C Y, Milankov K, Michalak M, Wilkins J, Dedhar S. Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin alpha-subunit-binding protein. J Cell Sci 1994; 107: 589-600.
    • (1994) J Cell Sci , vol.107 , pp. 589-600
    • Leung-Hagesteijn, C.Y.1    Milankov, K.2    Michalak, M.3    Wilkins, J.4    Dedhar, S.5
  • 19
    • 0029090122 scopus 로고
    • Inducible interaction of integrin α2β1 with calreticulin. Dependence on the activation state of the integrin
    • Coppolino M, Leung-Hagesteijn C, Dedhar S, Wilkins J. Inducible interaction of integrin α2β1 with calreticulin. Dependence on the activation state of the integrin. J Biol Chem 1995; 270: 23132-8.
    • (1995) J Biol Chem , vol.270 , pp. 23132-23138
    • Coppolino, M.1    Leung-Hagesteijn, C.2    Dedhar, S.3    Wilkins, J.4
  • 20
    • 0030459614 scopus 로고    scopus 로고
    • Calreticulin modulates cell adhesiveness via regulation of vinculin expression
    • Opas M, Szewczenko-Pawlikowski M, Jass G K, Mesaeli NMM. Calreticulin modulates cell adhesiveness via regulation of vinculin expression. J Cell Biol 1996; 135: 1913-23.
    • (1996) J Cell Biol , vol.135 , pp. 1913-1923
    • Opas, M.1    Szewczenko-Pawlikowski, M.2    Jass, G.K.3    Mesaeli, N.M.M.4
  • 23
    • 0025886562 scopus 로고
    • A new procedure for the separation of protein Z, prothrombin fragment 1. 2 and calreticulin from human plasma
    • Sueyoshi T, McMullen B A, Marnell L L, Du Clos T W, Kisiel W. A new procedure for the separation of protein Z, prothrombin fragment 1.2 and calreticulin from human plasma. Thromb Res 1991; 63: 569-75.
    • (1991) Thromb Res , vol.63 , pp. 569-575
    • Sueyoshi, T.1    McMullen, B.A.2    Marnell, L.L.3    Du Clos, T.W.4    Kisiel, W.5
  • 24
    • 0018231982 scopus 로고
    • The platelet dense tubular system: Its relationship to prostaglandin synthesis and calcium flux
    • Gerrard J M, White J G, Peterson DA. The platelet dense tubular system: its relationship to prostaglandin synthesis and calcium flux. Thromb Haemost 1978; 40: 224-31.
    • (1978) Thromb Haemost , vol.40 , pp. 224-231
    • Gerrard, J.M.1    White, J.G.2    Peterson, D.A.3
  • 25
    • 0033562951 scopus 로고    scopus 로고
    • Ligand-specific, transient interaction between integrins and calreticulin during cell adhesion to extracellular matrix proteins is dependent upon phosphorylation/dephosphorylation events
    • Coppolino M G, Dedhar S. Ligand-specific, transient interaction between integrins and calreticulin during cell adhesion to extracellular matrix proteins is dependent upon phosphorylation/dephosphorylation events. Biochem J 1999; 340: 41-50.
    • (1999) Biochem J , vol.340 , pp. 41-50
    • Coppolino, M.G.1    Dedhar, S.2
  • 26
    • 0034121267 scopus 로고    scopus 로고
    • Talin controls the exit of the integrin α5β1 from an early compartment of the secretory pathway
    • Martel V, Vignoud L, Dupe S, Frachet P, Block M R, Albiges-Rizo C. Talin controls the exit of the integrin α5β1 from an early compartment of the secretory pathway. J Cell Sci 2000; 113: 1951-61.
    • (2000) J Cell Sci , vol.113 , pp. 1951-1961
    • Martel, V.1    Vignoud, L.2    Dupe, S.3    Frachet, P.4    Block, M.R.5    Albiges-Rizo, C.6
  • 27
    • 0017350087 scopus 로고
    • Platelet plasma membrane glycoproteins. Evidence for the presence of nonequivalent disulfide bonds using nonreduced-reduced two-dimensional gel electrophoresis
    • Phillips D R, Agin PP. Platelet plasma membrane glycoproteins. Evidence for the presence of nonequivalent disulfide bonds using nonreduced-reduced two-dimensional gel electrophoresis. J Biol Chem 1977; 252: 2121-6.
    • (1977) J Biol Chem , vol.252 , pp. 2121-2126
    • Phillips, D.R.1    Agin, P.P.2
  • 30
    • 0030696936 scopus 로고    scopus 로고
    • Analysis of the tetraspanin CD9-integrin αIIbβ3 (GPIIb-IIIa) complex in platelet membranes and transfected cells
    • Indig F E, Diaz-Gonzalez F, Ginsberg MH. Analysis of the tetraspanin CD9-integrin αIIbβ3 (GPIIb-IIIa) complex in platelet membranes and transfected cells. Biochem J 1997; 327: 291-8.
    • (1997) Biochem J , vol.327 , pp. 291-298
    • Indig, F.E.1    Diaz-Gonzalez, F.2    Ginsberg, M.H.3
  • 31
    • 0033559816 scopus 로고    scopus 로고
    • Activation of integrin-β3-associated syk in platelets
    • Sarkar S, Rooney M M, Lord ST. Activation of integrin-β3-associated syk in platelets. Biochem J 1999; 338: 677-80.
    • (1999) Biochem J , vol.338 , pp. 677-680
    • Sarkar, S.1    Rooney, M.M.2    Lord, S.T.3
  • 32
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin: A transmembrane linkage
    • Horwitz A, Duggan K, Buck C, Beckerle M C, Burridge K. Interaction of plasma membrane fibronectin receptor with talin: a transmembrane linkage. Nature 1986; 320: 531-3.
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 34
    • 0034646876 scopus 로고    scopus 로고
    • Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
    • Molinari M, Helenius A. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 2000; 288: 331-3.
    • (2000) Science , vol.288 , pp. 331-333
    • Molinari, M.1    Helenius, A.2
  • 35
    • 0037041030 scopus 로고    scopus 로고
    • The small GTPase Rac3 interacts with the integrin-binding protein CIB and promotes integrin αIIbβ3-mediated adhesion and spreading
    • Haataja L, Kaartinen V, Groffen J, Heisterkamp N. The small GTPase Rac3 interacts with the integrin-binding protein CIB and promotes integrin αIIbβ3-mediated adhesion and spreading. J Biol Chem 2002; 277: 8321-8.
    • (2002) J Biol Chem , vol.277 , pp. 8321-8328
    • Haataja, L.1    Kaartinen, V.2    Groffen, J.3    Heisterkamp, N.4
  • 38
    • 0034652205 scopus 로고    scopus 로고
    • Structural basis for integrin activation by the cytoplasmic tail of the αIIb subunit
    • Vinogradova O, Haas T, Plow E F, Qin J. Structural basis for integrin activation by the cytoplasmic tail of the αIIb subunit. Proc Natl Acad Sci USA 2000; 97: 1450-5.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1450-1455
    • Vinogradova, O.1    Haas, T.2    Plow, E.F.3    Qin, J.4
  • 39
    • 0033546169 scopus 로고    scopus 로고
    • Divalent cations differentially regulate integrin αIIb cytoplasmic tail binding to β3 and to calcium- And integrin-binding protein
    • Vallar L, Melchior C, Plancon S, Drobecq H, Lippens G, Regnault V, Kieffer N. Divalent cations differentially regulate integrin αIIb cytoplasmic tail binding to β3 and to calcium-and integrin-binding protein. J Biol Chem 1999; 274: 17257-66.
    • (1999) J Biol Chem , vol.274 , pp. 17257-17266
    • Vallar, L.1    Melchior, C.2    Plancon, S.3    Drobecq, H.4    Lippens, G.5    Regnault, V.6    Kieffer, N.7
  • 40
    • 0025222804 scopus 로고
    • A conformation-dependent epitope of human platelet glycoprotein IIIa
    • Kouns W C, Wall C D, White M M, Fox C F, Jennings LK. A conformation-dependent epitope of human platelet glycoprotein IIIa. J Biol Chem 1990; 265: 20594-601.
    • (1990) J Biol Chem , vol.265 , pp. 20594-20601
    • Kouns, W.C.1    Wall, C.D.2    White, M.M.3    Fox, C.F.4    Jennings, L.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.