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Volumn 441, Issue 4, 2013, Pages 988-993

Disease-associated single amino acid mutation in the calf-1 domain of integrin α3 leads to defects in its processing and cell surface expression

Author keywords

Basement membrane; CD151; Glycosylation; Laminin; Posttranslational modification; Tetraspanin

Indexed keywords

ALPHA3 INTEGRIN; ARGININE; BETA1 INTEGRIN; CD151 ANTIGEN; GLUTAMIC ACID; GLUTAMINE; MUTANT PROTEIN; PROLINE; TETRASPANIN;

EID: 84888823769     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2013.11.003     Document Type: Article
Times cited : (13)

References (19)
  • 1
    • 33645380797 scopus 로고    scopus 로고
    • Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant α3β1, α6β1, α7β1 and α6β4 integrins
    • Nishiuchi R., Takagi J., Hayashi M., Ido H., Yagi Y., Sanzen N., Tsuji T., Yamada M., Sekiguchi K. Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant α3β1, α6β1, α7β1 and α6β4 integrins. Matrix Biol. 2006, 25:189-197.
    • (2006) Matrix Biol. , vol.25 , pp. 189-197
    • Nishiuchi, R.1    Takagi, J.2    Hayashi, M.3    Ido, H.4    Yagi, Y.5    Sanzen, N.6    Tsuji, T.7    Yamada, M.8    Sekiguchi, K.9
  • 3
    • 0034652182 scopus 로고    scopus 로고
    • Endoproteolytic processing of integrin pro-α subunits involves the redundant function of furin and proprotein convertase (PC) 5A, but not paired basic amino acid converting enzyme (PACE) 4, PC5B or PC7
    • Lissitzky J.C., Luis J., Munzer J.S., Benjannet S., Parat F., Chretien M., Marvaldi J., Seidah N.G. Endoproteolytic processing of integrin pro-α subunits involves the redundant function of furin and proprotein convertase (PC) 5A, but not paired basic amino acid converting enzyme (PACE) 4, PC5B or PC7. Biochem. J. 2000, 346:133-138.
    • (2000) Biochem. J. , vol.346 , pp. 133-138
    • Lissitzky, J.C.1    Luis, J.2    Munzer, J.S.3    Benjannet, S.4    Parat, F.5    Chretien, M.6    Marvaldi, J.7    Seidah, N.G.8
  • 8
    • 84878772614 scopus 로고    scopus 로고
    • Substrate-attached materials are enriched with tetraspanins and are analogous to the structures associated with rear-end retraction in migrating cells
    • Yamada M., Mugnai G., Serada S., Yagi Y., Naka T., Sekiguchi K. Substrate-attached materials are enriched with tetraspanins and are analogous to the structures associated with rear-end retraction in migrating cells. Cell Adhes. Migr. 2013, 7:304-314.
    • (2013) Cell Adhes. Migr. , vol.7 , pp. 304-314
    • Yamada, M.1    Mugnai, G.2    Serada, S.3    Yagi, Y.4    Naka, T.5    Sekiguchi, K.6
  • 10
    • 58149150978 scopus 로고    scopus 로고
    • Probing the interaction of tetraspanin CD151 with integrin α3β1 using a panel of monoclonal antibodies with distinct reactivities toward the CD151-integrin α3β1 complex
    • Yamada M., Tamura Y., Sanzen N., Sato-Nishiuchi R., Hasegawa H., Ashman L.K., Rubinstein E., Yanez-Mo M., Sanchez-Madrid F., Sekiguchi K. Probing the interaction of tetraspanin CD151 with integrin α3β1 using a panel of monoclonal antibodies with distinct reactivities toward the CD151-integrin α3β1 complex. Biochem. J. 2008, 415:417-427.
    • (2008) Biochem. J. , vol.415 , pp. 417-427
    • Yamada, M.1    Tamura, Y.2    Sanzen, N.3    Sato-Nishiuchi, R.4    Hasegawa, H.5    Ashman, L.K.6    Rubinstein, E.7    Yanez-Mo, M.8    Sanchez-Madrid, F.9    Sekiguchi, K.10
  • 13
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler M.E. Tetraspanin functions and associated microdomains. Nat. Rev. Mol. Cell Biol. 2005, 6:801-811.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 14
    • 77953064012 scopus 로고    scopus 로고
    • Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets
    • Stipp C.S. Laminin-binding integrins and their tetraspanin partners as potential antimetastatic targets. Expert Rev. Mol. Med. 2010, 12:e3.
    • (2010) Expert Rev. Mol. Med. , vol.12
    • Stipp, C.S.1
  • 15
    • 0034737471 scopus 로고    scopus 로고
    • Direct extracellular contact between integrin α3β1 and TM4SF protein CD151
    • Yauch R.L., Kazarov A.R., Desai B., Lee R.T., Hemler M.E. Direct extracellular contact between integrin α3β1 and TM4SF protein CD151. J. Biol. Chem. 2000, 275:9230-9238.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9230-9238
    • Yauch, R.L.1    Kazarov, A.R.2    Desai, B.3    Lee, R.T.4    Hemler, M.E.5
  • 16
    • 0345004833 scopus 로고    scopus 로고
    • Molecular genetic analysis of a compound heterozygote for the glycoprotein (GP) IIb gene associated with Glanzmann's thrombasthenia: disruption of the 674-687 disulfide bridge in GPIIb prevents surface exposure of GPIIb-IIIa complexes
    • Gonzalez-Manchon C., Fernandez-Pinel M., Arias-Salgado E.G., Ferrer M., Alvarez M.V., Garcia-Munoz S., Ayuso M.S., Parrilla R. Molecular genetic analysis of a compound heterozygote for the glycoprotein (GP) IIb gene associated with Glanzmann's thrombasthenia: disruption of the 674-687 disulfide bridge in GPIIb prevents surface exposure of GPIIb-IIIa complexes. Blood 1999, 93:866-875.
    • (1999) Blood , vol.93 , pp. 866-875
    • Gonzalez-Manchon, C.1    Fernandez-Pinel, M.2    Arias-Salgado, E.G.3    Ferrer, M.4    Alvarez, M.V.5    Garcia-Munoz, S.6    Ayuso, M.S.7    Parrilla, R.8
  • 17
    • 0037777629 scopus 로고    scopus 로고
    • Major mutations in calf-1 and calf-2 domains of glycoprotein IIb in patients with Glanzmann thrombasthenia enable GPIIb/IIIa complex formation, but impair its transport from the endoplasmic reticulum to the Golgi apparatus
    • Rosenberg N., Yatuv R., Sobolev V., Peretz H., Zivelin A., Seligsohn U. Major mutations in calf-1 and calf-2 domains of glycoprotein IIb in patients with Glanzmann thrombasthenia enable GPIIb/IIIa complex formation, but impair its transport from the endoplasmic reticulum to the Golgi apparatus. Blood 2003, 101:4808-4815.
    • (2003) Blood , vol.101 , pp. 4808-4815
    • Rosenberg, N.1    Yatuv, R.2    Sobolev, V.3    Peretz, H.4    Zivelin, A.5    Seligsohn, U.6
  • 18
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur M.W., Thornton J.M. Influence of proline residues on protein conformation. J. Mol. Biol. 1991, 218:397-412.
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 19
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: targeting proteins for degradation in the endoplasmic reticulum
    • Smith M.H., Ploegh H.L., Weissman J.S. Road to ruin: targeting proteins for degradation in the endoplasmic reticulum. Science 2011, 334:1086-1090.
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.