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Volumn 28, Issue 2, 2003, Pages 106-112

Functional domains in tetraspanin proteins

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; TETRASPANIN;

EID: 0037310188     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(02)00014-2     Document Type: Review
Times cited : (387)

References (56)
  • 1
    • 0033964768 scopus 로고    scopus 로고
    • Severely reduced female fertility in CD9-deficient mice
    • Le Naour F., et al. Severely reduced female fertility in CD9-deficient mice. Science. 287:2000;319-321.
    • (2000) Science , vol.287 , pp. 319-321
    • Le Naour, F.1
  • 2
    • 0033958932 scopus 로고    scopus 로고
    • Requirement of CD9 on the egg plasma membrane for fertilization
    • Miyado K., et al. Requirement of CD9 on the egg plasma membrane for fertilization. Science. 287:2000;321-324.
    • (2000) Science , vol.287 , pp. 321-324
    • Miyado, K.1
  • 3
    • 0034091646 scopus 로고    scopus 로고
    • The gamete fusion process is defective in eggs of Cd9-deficient mice
    • Kaji K., et al. The gamete fusion process is defective in eggs of Cd9-deficient mice. Nat. Genet. 24:2000;279-282.
    • (2000) Nat. Genet. , vol.24 , pp. 279-282
    • Kaji, K.1
  • 4
    • 0031895778 scopus 로고    scopus 로고
    • CD81 (TAPA-1): A molecule involved in signal transduction and cell adhesion in the immune system
    • Levy S., et al. CD81 (TAPA-1): a molecule involved in signal transduction and cell adhesion in the immune system. Annu. Rev. Immunol. 16:1998;89-109.
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 89-109
    • Levy, S.1
  • 5
    • 85012505212 scopus 로고    scopus 로고
    • Tetraspanins and malignancy
    • Boucheix C., et al. Tetraspanins and malignancy. Exp. Rev. Mol. 2001;1-17. http://www-ermm.cbcu.cam.ac.uk/01002381h.htm.
    • (2001) Exp. Rev. Mol. , pp. 1-17
    • Boucheix, C.1
  • 6
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: More than meets the eye
    • Berditchevski F. Complexes of tetraspanins with integrins: more than meets the eye. J. Cell Sci. 114:2001;4143-4151.
    • (2001) J. Cell Sci. , vol.114 , pp. 4143-4151
    • Berditchevski, F.1
  • 7
    • 0035945363 scopus 로고    scopus 로고
    • Specific tetraspanin functions
    • Hemler M.E. Specific tetraspanin functions. J. Cell Biol. 155:2001;1103-1107.
    • (2001) J. Cell Biol. , vol.155 , pp. 1103-1107
    • Hemler, M.E.1
  • 8
    • 0035376066 scopus 로고    scopus 로고
    • Tetraspanins and intercellular interactions
    • Yánez-Mó M., et al. Tetraspanins and intercellular interactions. Microcirculation. 8:2001;153-168.
    • (2001) Microcirculation , vol.8 , pp. 153-168
    • Yánez-Mó, M.1
  • 10
    • 0031720629 scopus 로고    scopus 로고
    • Integrin-associated proteins
    • Hemler M.E. Integrin-associated proteins. Curr. Opin. Cell Biol. 10:1998;578-585.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 578-585
    • Hemler, M.E.1
  • 11
    • 0037072814 scopus 로고    scopus 로고
    • Tetraspanin CD9 is a 'proteolipid' and its interaction with α3 integrin in microdomain is promoted by GM3 ganglioside, leading to inhibition of laminin-5-dependent cell motility
    • Kawakami Y., et al. Tetraspanin CD9 is a 'proteolipid' and its interaction with α3 integrin in microdomain is promoted by GM3 ganglioside, leading to inhibition of laminin-5-dependent cell motility. J. Biol. Chem. 277:2002;34349-34358.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34349-34358
    • Kawakami, Y.1
  • 12
    • 0030696936 scopus 로고    scopus 로고
    • Analysis of the tetraspanin CD9-integrin αIIbβ3 (GPIIb-IIIa) complex in platelet membranes and transfected cells
    • Indig F.E., et al. Analysis of the tetraspanin CD9-integrin αIIbβ3 (GPIIb-IIIa) complex in platelet membranes and transfected cells. Biochem. J. 327:1997;291-298.
    • (1997) Biochem. J. , vol.327 , pp. 291-298
    • Indig, F.E.1
  • 13
    • 0031660652 scopus 로고    scopus 로고
    • Highly stoichiometric, stable and specific association of integrin α3β1 with CD151 provides a major link to phosphatidylinositol 4-kinase and may regulate cell migration
    • Yauch R.L., et al. Highly stoichiometric, stable and specific association of integrin α3β1 with CD151 provides a major link to phosphatidylinositol 4-kinase and may regulate cell migration. Mol. Biol. Cell. 9:1998;2751-2765.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2751-2765
    • Yauch, R.L.1
  • 14
    • 0031018172 scopus 로고    scopus 로고
    • A novel link between integrins, TM4SF proteins (CD63, CD81) and phosphatidylinositol 4-kinase
    • Berditchevski F., et al. A novel link between integrins, TM4SF proteins (CD63, CD81) and phosphatidylinositol 4-kinase. J. Biol. Chem. 272:1997;2595-2598.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2595-2598
    • Berditchevski, F.1
  • 15
    • 0035816663 scopus 로고    scopus 로고
    • TM4SF proteins associate with activated PKC and Link PKC to specific β1 integrins
    • Zhang X.A., et al. TM4SF proteins associate with activated PKC and Link PKC to specific β1 integrins. J. Biol. Chem. 276:2001;25005-25013.
    • (2001) J. Biol. Chem. , vol.276 , pp. 25005-25013
    • Zhang, X.A.1
  • 16
    • 0035896648 scopus 로고    scopus 로고
    • Evaluation of prototype TM4SF protein complexes and their relation to lipid rafts
    • Claas C., et al. Evaluation of prototype TM4SF protein complexes and their relation to lipid rafts. J. Biol. Chem. 276:2001;7974-7984.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7974-7984
    • Claas, C.1
  • 17
    • 0036290481 scopus 로고    scopus 로고
    • Localization of uroplakin Ia, the urothelial receptor for bacterial adhesin FimH, on the six inner domains of the 16 nm urothelial plaque particle
    • Min G., et al. Localization of uroplakin Ia, the urothelial receptor for bacterial adhesin FimH, on the six inner domains of the 16 nm urothelial plaque particle. J. Mol. Biol. 317:2002;697-706.
    • (2002) J. Mol. Biol. , vol.317 , pp. 697-706
    • Min, G.1
  • 18
    • 0035940960 scopus 로고    scopus 로고
    • Structure of the major membrane protein complex from urinary bladder epithelial cells by cryo-electron crystallography
    • Oostergetel G.T., et al. Structure of the major membrane protein complex from urinary bladder epithelial cells by cryo-electron crystallography. J. Mol. Biol. 314:2001;245-252.
    • (2001) J. Mol. Biol. , vol.314 , pp. 245-252
    • Oostergetel, G.T.1
  • 19
    • 0035895876 scopus 로고    scopus 로고
    • FPRP: A major, highly stoichiometric, highly specific CD81 and CD9-associated protein
    • Stipp C.S., et al. FPRP: A major, highly stoichiometric, highly specific CD81 and CD9-associated protein. J. Biol. Chem. 276:2001;4853-4862.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4853-4862
    • Stipp, C.S.1
  • 20
    • 0035798537 scopus 로고    scopus 로고
    • EWI-2 is a major CD9 and CD81 partner, and member of a novel Ig protein subfamily
    • Stipp C.S., et al. EWI-2 is a major CD9 and CD81 partner, and member of a novel Ig protein subfamily. J. Biol. Chem. 276:2001;40545-40554.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40545-40554
    • Stipp, C.S.1
  • 21
    • 0035958026 scopus 로고    scopus 로고
    • The major CD9 and CD81 molecular partner. Identification and characterization of the complexes
    • Charrin S., et al. The major CD9 and CD81 molecular partner. Identification and characterization of the complexes. J. Biol. Chem. 276:2001;14329-14337.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14329-14337
    • Charrin, S.1
  • 22
    • 0035500912 scopus 로고    scopus 로고
    • Pgrl is a major CD81-associated protein on lymphocytes and distinguishes a new family of cell surface proteins
    • Clark K.L., et al. Pgrl is a major CD81-associated protein on lymphocytes and distinguishes a new family of cell surface proteins. J. Immunol. 167:2001;5115-5121.
    • (2001) J. Immunol. , vol.167 , pp. 5115-5121
    • Clark, K.L.1
  • 23
    • 0037087710 scopus 로고    scopus 로고
    • Association of the tetraspanin CD151 with the laminin-binding integrins α3β1, α6β1, α6β4 and α7β1 in cells in culture and in vivo
    • Sterk L.M., et al. Association of the tetraspanin CD151 with the laminin-binding integrins α3β1, α6β1, α6β4 and α7β1 in cells in culture and in vivo. J. Cell Sci. 115:2002;1161-1173.
    • (2002) J. Cell Sci. , vol.115 , pp. 1161-1173
    • Sterk, L.M.1
  • 24
    • 0032482216 scopus 로고    scopus 로고
    • Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with α3β1 integrin localized at endothelial lateral junctions
    • Yánez-Mó M., et al. Regulation of endothelial cell motility by complexes of tetraspan molecules CD81/TAPA-1 and CD151/PETA-3 with α3β1 integrin localized at endothelial lateral junctions. J. Cell Biol. 141:1998;791-804.
    • (1998) J. Cell Biol. , vol.141 , pp. 791-804
    • Yánez-Mó, M.1
  • 25
    • 0032948124 scopus 로고    scopus 로고
    • PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function
    • Sincock P.M., et al. PETA-3/CD151, a member of the transmembrane 4 superfamily, is localised to the plasma membrane and endocytic system of endothelial cells, associates with multiple integrins and modulates cell function. J. Cell Sci. 112:1999;833-844.
    • (1999) J. Cell Sci. , vol.112 , pp. 833-844
    • Sincock, P.M.1
  • 26
    • 0034737471 scopus 로고    scopus 로고
    • Direct extracellular contact between integrin α3β1 and TM4SF protein CD151
    • Yauch R.L., et al. Direct extracellular contact between integrin α3β1 and TM4SF protein CD151. J. Biol. Chem. 275:2000;9230-9238.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9230-9238
    • Yauch, R.L.1
  • 27
    • 0035798702 scopus 로고    scopus 로고
    • Analysis of the CD151-α3β1 integrin and CD151-tetraspanin interactions by mutagenesis
    • Berditchevski F., et al. Analysis of the CD151-α3β1 integrin and CD151-tetraspanin interactions by mutagenesis. J. Biol. Chem. 276:2001;41165-41174.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41165-41174
    • Berditchevski, F.1
  • 28
    • 0037144837 scopus 로고    scopus 로고
    • An extracellular site on tetraspanin CD151 determines α3 and α6 integrin-dependent cellular morphology
    • Kazarov A.R., et al. An extracellular site on tetraspanin CD151 determines α3 and α6 integrin-dependent cellular morphology. J. Cell Biol. 158:2002;1299-1309.
    • (2002) J. Cell Biol. , vol.158 , pp. 1299-1309
    • Kazarov, A.R.1
  • 29
    • 0036151461 scopus 로고    scopus 로고
    • Function of the tetraspanin CD151-a6b1 integrin complex during cellular morphogenesis
    • Zhang X.A., et al. Function of the tetraspanin CD151-a6b1 integrin complex during cellular morphogenesis. Mol. Biol. Cell. 13:2002;1-11.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1-11
    • Zhang, X.A.1
  • 30
    • 0036198534 scopus 로고    scopus 로고
    • Palmitoylation of tetraspanin proteins: Modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology
    • Yang X., et al. Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology. Mol. Biol. Cell. 13:2002;767-781.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 767-781
    • Yang, X.1
  • 31
    • 0034792892 scopus 로고    scopus 로고
    • The small extracellular loop of CD81 is necessary for optimal surface expression of the large loop, a putative HCV receptor
    • Masciopinto F., et al. The small extracellular loop of CD81 is necessary for optimal surface expression of the large loop, a putative HCV receptor. Virus Res. 80:2001;1-10.
    • (2001) Virus Res. , vol.80 , pp. 1-10
    • Masciopinto, F.1
  • 32
    • 0035862964 scopus 로고    scopus 로고
    • CD81 extracellular domain 3D structure: Insight into the tetraspanin superfamily structural motifs
    • Kitadokoro K., et al. CD81 extracellular domain 3D structure: insight into the tetraspanin superfamily structural motifs. EMBO J. 20:2001;12-18.
    • (2001) EMBO J. , vol.20 , pp. 12-18
    • Kitadokoro, K.1
  • 33
    • 0035955657 scopus 로고    scopus 로고
    • Structure of the tetraspanin main extracellular domain. A partially conserved fold with a structurally variable domain insertion
    • Seigneuret M., et al. Structure of the tetraspanin main extracellular domain. A partially conserved fold with a structurally variable domain insertion. J. Biol. Chem. 276:2001;40055-40064.
    • (2001) J. Biol. Chem. , vol.276 , pp. 40055-40064
    • Seigneuret, M.1
  • 34
    • 18844463856 scopus 로고    scopus 로고
    • Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2
    • Higginbottom A., et al. Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2. J. Virol. 74:2000;3642-3649.
    • (2000) J. Virol. , vol.74 , pp. 3642-3649
    • Higginbottom, A.1
  • 35
    • 0036333987 scopus 로고    scopus 로고
    • Residues SFQ (173-175) in the large extracellular loop of CD9 are required for gamete fusion
    • Zhu G.Z., et al. Residues SFQ (173-175) in the large extracellular loop of CD9 are required for gamete fusion. Development. 129:2002;1995-2002.
    • (2002) Development , vol.129 , pp. 1995-2002
    • Zhu, G.Z.1
  • 36
    • 0028284810 scopus 로고
    • Heparin-binding EGF-like growth factor, which acts as a diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which upregulates functional receptors and diphtheria toxin sensitivity
    • Iwamoto R., et al. Heparin-binding EGF-like growth factor, which acts as a diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which upregulates functional receptors and diphtheria toxin sensitivity. EMBO J. 13:1994;2322-2330.
    • (1994) EMBO J. , vol.13 , pp. 2322-2330
    • Iwamoto, R.1
  • 37
    • 0028963636 scopus 로고
    • The membrane protein CD9/DRAP27 potentiates the juxtacrine growth factor activity of the membrane-anchored heparin-binding EGF-like growth factor
    • Higashiyama S., et al. The membrane protein CD9/DRAP27 potentiates the juxtacrine growth factor activity of the membrane-anchored heparin-binding EGF-like growth factor. J. Cell Biol. 128:1995;929-938.
    • (1995) J. Cell Biol. , vol.128 , pp. 929-938
    • Higashiyama, S.1
  • 38
    • 0035861966 scopus 로고    scopus 로고
    • CD9 amino acids critical for upregulation of diphtheria toxin binding
    • Hasuwa H., et al. CD9 amino acids critical for upregulation of diphtheria toxin binding. Biochem. Biophys. Res. Commun. 289:2001;782-790.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 782-790
    • Hasuwa, H.1
  • 39
    • 0034614938 scopus 로고    scopus 로고
    • The tetraspanin CD9 associates with transmembrane TGF-α and regulates TGF-α-induced EGF receptor activation and cell proliferation
    • Shi W., et al. The tetraspanin CD9 associates with transmembrane TGF-α and regulates TGF-α-induced EGF receptor activation and cell proliferation. J. Cell Biol. 148:2000;591-602.
    • (2000) J. Cell Biol. , vol.148 , pp. 591-602
    • Shi, W.1
  • 40
    • 0033968407 scopus 로고    scopus 로고
    • A new gene involved in X-linked mental retardation identified by analysis of an X;2 balanced translocation
    • Zemni R., et al. A new gene involved in X-linked mental retardation identified by analysis of an X;2 balanced translocation. Nat. Genet. 24:2000;167-170.
    • (2000) Nat. Genet. , vol.24 , pp. 167-170
    • Zemni, R.1
  • 41
    • 0031772105 scopus 로고    scopus 로고
    • The role of the peripherin/RDS gene in retinal dystrophies
    • Kohl S., et al. The role of the peripherin/RDS gene in retinal dystrophies. Acta Anat. (Basel). 162:1998;75-84.
    • (1998) Acta Anat. (Basel) , vol.162 , pp. 75-84
    • Kohl, S.1
  • 42
    • 0007949690 scopus 로고    scopus 로고
    • Interhelical hydrogen bonding drives strong interactions in membrane proteins
    • Zhou F.X., et al. Interhelical hydrogen bonding drives strong interactions in membrane proteins. Nat. Struct. Biol. 7:2000;154-160.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 154-160
    • Zhou, F.X.1
  • 43
    • 0035969998 scopus 로고    scopus 로고
    • Polar side chains drive the association of model transmembrane peptides
    • Gratkowski H., et al. Polar side chains drive the association of model transmembrane peptides. Proc. Natl. Acad. Sci. U. S. A. 98:2001;880-885.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 880-885
    • Gratkowski, H.1
  • 44
    • 0035162539 scopus 로고    scopus 로고
    • KAI1, a prostate metastasis suppressor: Prediction of solvated structure and interactions with binding partners; Integrins, cadherins, and cell-surface receptor proteins
    • Bienstock R.J., Barrett J.C. KAI1, a prostate metastasis suppressor: prediction of solvated structure and interactions with binding partners; integrins, cadherins, and cell-surface receptor proteins. Mol. Carcinog. 32:2001;139-153.
    • (2001) Mol. Carcinog. , vol.32 , pp. 139-153
    • Bienstock, R.J.1    Barrett, J.C.2
  • 45
    • 0035979146 scopus 로고    scopus 로고
    • The Cα-H.O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
    • Senes A., et al. The Cα-H.O hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions. Proc. Natl. Acad. Sci. U. S. A. 98:2001;9056-9061.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 9056-9061
    • Senes, A.1
  • 46
    • 0035872923 scopus 로고    scopus 로고
    • Quality control of transmembrane domain assembly in the tetraspanin CD82
    • Cannon K.S., Cresswell P. Quality control of transmembrane domain assembly in the tetraspanin CD82. EMBO J. 20:2001;2443-2453.
    • (2001) EMBO J. , vol.20 , pp. 2443-2453
    • Cannon, K.S.1    Cresswell, P.2
  • 47
    • 0037020085 scopus 로고    scopus 로고
    • Expression of the palmitoylation-deficient CD151 weakens the association of (3β1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signaling
    • Berditchevski F., et al. Expression of the palmitoylation-deficient CD151 weakens the association of (3β1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signaling. J. Biol. Chem. 277:2002;36991-37000.
    • (2002) J. Biol. Chem. , vol.277 , pp. 36991-37000
    • Berditchevski, F.1
  • 48
    • 0037051906 scopus 로고    scopus 로고
    • Differential stability of tetraspanin/tetraspanin interactions: Role of palmitoylation
    • Charrin S., et al. Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation. FEBS Lett. 516:2002;139-144.
    • (2002) FEBS Lett. , vol.516 , pp. 139-144
    • Charrin, S.1
  • 49
    • 0032497835 scopus 로고    scopus 로고
    • Signaling functions of protein palmitoylation
    • Dunphy J.T., Linder M.E. Signaling functions of protein palmitoylation. Biochim. Biophys. Acta. 1436:1998;245-261.
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 245-261
    • Dunphy, J.T.1    Linder, M.E.2
  • 50
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh M.D. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim. Biophys. Acta. 1451:1999;1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 51
    • 0034141469 scopus 로고    scopus 로고
    • Non-CD28 costimulatory molecules present in T cell rafts induce T cell costimulation by enhancing the association of TCR with rafts
    • Yashiro-Ohtani Y., et al. Non-CD28 costimulatory molecules present in T cell rafts induce T cell costimulation by enhancing the association of TCR with rafts. J. Immunol. 164:2000;1251-1259.
    • (2000) J. Immunol. , vol.164 , pp. 1251-1259
    • Yashiro-Ohtani, Y.1
  • 52
    • 0036196266 scopus 로고    scopus 로고
    • Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomes
    • Rous B.A., et al. Role of adaptor complex AP-3 in targeting wild-type and mutated CD63 to lysosomes. Mol. Biol. Cell. 13:2002;1071-1082.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1071-1082
    • Rous, B.A.1
  • 53
    • 0033620656 scopus 로고    scopus 로고
    • Molecular bases for the recognition of tyrosine-based sorting signals
    • Bonifacino J.S., Dell-Angelica E.C. Molecular bases for the recognition of tyrosine-based sorting signals. J. Cell Biol. 145:1999;923-926.
    • (1999) J. Cell Biol. , vol.145 , pp. 923-926
    • Bonifacino, J.S.1    Dell-Angelica, E.C.2
  • 54
    • 0032493658 scopus 로고    scopus 로고
    • Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes
    • Escola J.M., et al. Selective enrichment of tetraspan proteins on the internal vesicles of multivesicular endosomes and on exosomes secreted by human B-lymphocytes. J. Biol. Chem. 273:1998;20121-20127.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20121-20127
    • Escola, J.M.1
  • 55
    • 0031739534 scopus 로고    scopus 로고
    • Signaling through the tetraspanin CD82 triggers its association with the cytoskeleton leading to sustained morphological changes and T cell activation
    • Lagaudriere-Gesbert C., et al. Signaling through the tetraspanin CD82 triggers its association with the cytoskeleton leading to sustained morphological changes and T cell activation. Eur. J. Immunol. 28:1998;4332-4344.
    • (1998) Eur. J. Immunol. , vol.28 , pp. 4332-4344
    • Lagaudriere-Gesbert, C.1
  • 56
    • 0035156603 scopus 로고    scopus 로고
    • Phosphorylation of a conserved integrin α3 chain QPSXXE motifs regulates signaling, motility, and cytoskeletal engagement
    • Zhang X.A., et al. Phosphorylation of a conserved integrin α3 chain QPSXXE motifs regulates signaling, motility, and cytoskeletal engagement. Mol. Biol. Cell. 12:2001;351-365.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 351-365
    • Zhang, X.A.1


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