메뉴 건너뛰기




Volumn , Issue , 2013, Pages 47-90

Organisation of the tetraspanin web

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84994737855     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-94-007-6070-7_3     Document Type: Chapter
Times cited : (8)

References (225)
  • 1
    • 35048816607 scopus 로고    scopus 로고
    • The transferrin receptor and the tetraspanin web molecules CD9, CD81, and CD9P-1 are differentially sorted into exosomes after TPA treatment of K562 cells
    • Abache T, Le Naour F, Planchón S, Harper F, Boucheix C, Rubinstein E (2007) The transferrin receptor and the tetraspanin web molecules CD9, CD81, and CD9P-1 are differentially sorted into exosomes after TPA treatment of K562 cells. J Cell Biochem 102:650-664
    • (2007) J Cell Biochem , vol.102 , pp. 650-664
    • Abache, T.1    Le Naour, F.2    Planchón, S.3    Harper, F.4    Boucheix, C.5    Rubinstein, E.6
  • 4
    • 0028057606 scopus 로고
    • Association of four antigens of the tetraspans family (CD37, CD53, TAPA-1, and R2/C33) with MHC class II glycoproteins
    • Angelisova P, Hilgert I, Horejsi V (1994) Association of four antigens of the tetraspans family (CD37, CD53, TAPA-1, and R2/C33) with MHC class II glycoproteins. Immunogenetics 39:249-256
    • (1994) Immunogenetics , vol.39 , pp. 249-256
    • Angelisova, P.1    Hilgert, I.2    Horejsi, V.3
  • 5
    • 0037097563 scopus 로고    scopus 로고
    • C-kit associated with the transmembrane 4 superfamily proteins constitutes a functionally distinct subunit in human hematopoietic progenitors
    • Anzai N, Lee Y, Youn BS, Fukuda S, Kim YJ, Mantel C, Akashi M, Broxmeyer HE (2002) C-kit associated with the transmembrane 4 superfamily proteins constitutes a functionally distinct subunit in human hematopoietic progenitors. Blood 99:4413-4421
    • (2002) Blood , vol.99 , pp. 4413-4421
    • Anzai, N.1    Lee, Y.2    Youn, B.S.3    Fukuda, S.4    Kim, Y.J.5    Mantel, C.6    Akashi, M.7    Broxmeyer, H.E.8
  • 8
    • 53149111544 scopus 로고    scopus 로고
    • Deletion of CD151 results in a strain-dependent glomerular disease due to severe alterations of the glomerular basement membrane
    • Baleato RM, Guthrie PL, Gubler MC, Ashman LK, Roselli S (2008) Deletion of CD151 results in a strain-dependent glomerular disease due to severe alterations of the glomerular basement membrane. Am J Pathol 173:927-937
    • (2008) Am J Pathol , vol.173 , pp. 927-937
    • Baleato, R.M.1    Guthrie, P.L.2    Gubler, M.C.3    Ashman, L.K.4    Roselli, S.5
  • 12
    • 65649133945 scopus 로고    scopus 로고
    • Palmitoylation controls the catalytic activity and subcellular distribution of phosphatidylinositol 4-kinase IIjalphaj
    • Barylko B, Mao YS, Wlodarski P, Jung G, Binns DD, Sun HQ, Yin HL, Albanesi JP (2009) Palmitoylation controls the catalytic activity and subcellular distribution of phosphatidylinositol 4-kinase IIjalphaj. J Biol Chem 284:9994-10003
    • (2009) J Biol Chem , vol.284 , pp. 9994-10003
    • Barylko, B.1    Mao, Y.S.2    Wlodarski, P.3    Jung, G.4    Binns, D.D.5    Sun, H.Q.6    Yin, H.L.7    Albanesi, J.P.8
  • 14
    • 0033950479 scopus 로고    scopus 로고
    • The tet-raspanin CD9 associates with the integrin alpha6beta4 in cultured human epidermal kerati-nocytes and is involved in cell motility
    • Baudoux B, Castanares-Zapatero D, Leclercq-Smekens M, Berna N, Poumay Y (2000) The tet-raspanin CD9 associates with the integrin alpha6beta4 in cultured human epidermal kerati-nocytes and is involved in cell motility. Eur J Cell Biol 79:41-51
    • (2000) Eur J Cell Biol , vol.79 , pp. 41-51
    • Baudoux, B.1    Castanares-Zapatero, D.2    Leclercq-Smekens, M.3    Berna, N.4    Poumay, Y.5
  • 15
    • 0026585492 scopus 로고
    • The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line
    • Bell GM, Seaman WE, Niemi EC, Imboden JB (1992) The OX-44 molecule couples to signaling pathways and is associated with CD2 on rat T lymphocytes and a natural killer cell line. J Exp Med 175:527-536
    • (1992) J Exp Med , vol.175 , pp. 527-536
    • Bell, G.M.1    Seaman, W.E.2    Niemi, E.C.3    Imboden, J.B.4
  • 16
    • 0029029882 scopus 로고
    • Specific association of CD63 with the VLA-3 and VLA-6 integrins
    • Berditchevski F, Bazzoni G, Hemler ME (1995) Specific association of CD63 with the VLA-3 and VLA-6 integrins. J Biol Chem 270:17784-17790
    • (1995) J Biol Chem , vol.270 , pp. 17784-17790
    • Berditchevski, F.1    Bazzoni, G.2    Hemler, M.E.3
  • 17
    • 0030062129 scopus 로고    scopus 로고
    • Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins)
    • Berditchevski F, Zutter MM, Hemler ME (1996) Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins). Mol BiolCell 7:193-207
    • (1996) Mol Biolcell , vol.7 , pp. 193-207
    • Berditchevski, F.1    Zutter, M.M.2    Hemler, M.E.3
  • 18
    • 0031018172 scopus 로고    scopus 로고
    • A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase
    • Berditchevski F, Tolias KF, Wong K, Carpenter CL, Hemler ME (1997) A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase. J Biol Chem 272:2595-2598
    • (1997) J Biol Chem , vol.272 , pp. 2595-2598
    • Berditchevski, F.1    Tolias, K.F.2    Wong, K.3    Carpenter, C.L.4    Hemler, M.E.5
  • 19
    • 0035798702 scopus 로고    scopus 로고
    • Analysis of the CD151-alpha3beta1 integrin and CD151-tetraspanin interactions by mutagenesis
    • Berditchevski F, Gilbert E, Griffiths MR, Fitter S, Ashman L, Jenner SJ (2001) Analysis of the CD151-alpha3beta1 integrin and CD151-tetraspanin interactions by mutagenesis. J Biol Chem 276:41165-41174
    • (2001) J Biol Chem , vol.276 , pp. 41165-41174
    • Berditchevski, F.1    Gilbert, E.2    Griffiths, M.R.3    Fitter, S.4    Ashman, L.5    Jenner, S.J.6
  • 20
    • 0037020085 scopus 로고    scopus 로고
    • Expression of the palmitoylation-deficient CD151 weakens the association of alpha 3 beta 1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signaling
    • Berditchevski F, Odintsova E, Sawada S, Gilbert E (2002) Expression of the palmitoylation-deficient CD151 weakens the association of alpha 3 beta 1 integrin with the tetraspanin-enriched microdomains and affects integrin-dependent signaling. J Biol Chem 277: 36991-37000
    • (2002) J Biol Chem , vol.277 , pp. 36991-37000
    • Berditchevski, F.1    Odintsova, E.2    Sawada, S.3    Gilbert, E.4
  • 21
    • 11244261160 scopus 로고    scopus 로고
    • ADAMs: Key components in EGFR signalling and development
    • Blobel CP (2005) ADAMs: key components in EGFR signalling and development. Nat Rev Mol Cell Biol 6:32-43
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 32-43
    • Blobel, C.P.1
  • 23
    • 0026758271 scopus 로고
    • The CD19/CD21 signal transducing complex of human B lymphocytes includes the target of antiproliferative antibody-1 and Leu-13 molecules
    • Bradbury LE, Kansas GS, Levy S, Evans RL, Tedder TF (1992) The CD19/CD21 signal transducing complex of human B lymphocytes includes the target of antiproliferative antibody-1 and Leu-13 molecules. J Immunol 149:2841-2850
    • (1992) J Immunol , vol.149 , pp. 2841-2850
    • Bradbury, L.E.1    Kansas, G.S.2    Levy, S.3    Evans, R.L.4    Tedder, T.F.5
  • 25
    • 0026587743 scopus 로고
    • CD19: Lowering the treshold for antigen receptor stimulation of B lymphocytes
    • Carter RH, Fearon DT (1992) CD19: lowering the treshold for antigen receptor stimulation of B lymphocytes. Science 256:105-107
    • (1992) Science , vol.256 , pp. 105-107
    • Carter, R.H.1    Fearon, D.T.2
  • 26
    • 34948874257 scopus 로고    scopus 로고
    • Tetraspanin CD81 is required for the alpha v beta5-integrin-dependent particle-binding step of RPE phagocytosis
    • Chang Y, Finnemann SC (2007) Tetraspanin CD81 is required for the alpha v beta5-integrin-dependent particle-binding step of RPE phagocytosis. J Cell Sci 120:3053-3063
    • (2007) J Cell Sci , vol.120 , pp. 3053-3063
    • Chang, Y.1    Finnemann, S.C.2
  • 27
    • 32844474692 scopus 로고    scopus 로고
    • Role of ERM (Ezrin-Radixin-Moesin) proteins in T lymphocyte polarization, immune synapse formation and in T cell receptor-mediated signaling
    • Charrin S, Alcover A (2006) Role of ERM (Ezrin-Radixin-Moesin) proteins in T lymphocyte polarization, immune synapse formation and in T cell receptor-mediated signaling. Front Biosci 11:1987-1997
    • (2006) Front Biosci , vol.11 , pp. 1987-1997
    • Charrin, S.1    Alcover, A.2
  • 29
    • 0037051906 scopus 로고    scopus 로고
    • Differential stability of tetraspanin/tetraspanin interactions: Role of palmitoylation
    • Charrin S, Manie S, Oualid M, Billard M, Boucheix C, Rubinstein E (2002) Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation. FEBS Lett 516:139-144
    • (2002) FEBS Lett , vol.516 , pp. 139-144
    • Charrin, S.1    Manie, S.2    Oualid, M.3    Billard, M.4    Boucheix, C.5    Rubinstein, E.6
  • 36
    • 33645220951 scopus 로고    scopus 로고
    • Dissociation of the complex between CD151 and laminin-binding integrins permits migration of epithelial cells
    • Chometon G, Zhang ZG, Rubinstein E, Boucheix C, Mauch C, Aumailley M (2006) Dissociation of the complex between CD151 and laminin-binding integrins permits migration of epithelial cells. Exp Cell Res 312:983-995
    • (2006) Exp Cell Res , vol.312 , pp. 983-995
    • Chometon, G.1    Zhang, Z.G.2    Rubinstein, E.3    Boucheix, C.4    Mauch, C.5    Aumailley, M.6
  • 37
    • 0035896648 scopus 로고    scopus 로고
    • Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts
    • Claas C, Stipp CS, Hemler ME (2001) Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts. J Biol Chem 276:7974-7984
    • (2001) J Biol Chem , vol.276 , pp. 7974-7984
    • Claas, C.1    Stipp, C.S.2    Hemler, M.E.3
  • 39
    • 0035500912 scopus 로고    scopus 로고
    • Pgrl is a major cd81-associated protein on lymphocytes and distinguishes a new family of cell surface proteins
    • Clark KL, Zeng Z, Langford AL, Bowen SM, Todd SC (2001) Pgrl is a major cd81-associated protein on lymphocytes and distinguishes a new family of cell surface proteins. J Immunol 167:5115-5121
    • (2001) J Immunol , vol.167 , pp. 5115-5121
    • Clark, K.L.1    Zeng, Z.2    Langford, A.L.3    Bowen, S.M.4    Todd, S.C.5
  • 43
    • 19644364809 scopus 로고    scopus 로고
    • CD63 interacts with the carboxy terminus of the colonic H +-K +-ATPase to decrease [corrected] plasma membrane localization and 86Rb + uptake
    • Codina J, Li J, DuBose TD Jr (2005) CD63 interacts with the carboxy terminus of the colonic H +-K +-ATPase to decrease [corrected] plasma membrane localization and 86Rb + uptake. Am J Physiol Cell Physiol 288:C1279-C1286
    • (2005) Am J Physiol Cell Physiol , vol.288 , pp. C1279-C1286
    • Codina, J.1    Li, J.2    Dubose, T.D.3
  • 47
    • 9444291849 scopus 로고    scopus 로고
    • Tetraspanin CD82 controls the association of cholesterol-dependent microdomains with the actin cytoskeleton in T lymphocytes: Relevance to co-stimulation
    • Delaguillaumie A, Harriague J, Kohanna S, Bismuth G, Rubinstein E, Seigneuret M, Conjeaud H (2004) Tetraspanin CD82 controls the association of cholesterol-dependent microdomains with the actin cytoskeleton in T lymphocytes: relevance to co-stimulation. J Cell Sci 117: 5269-5282
    • (2004) J Cell Sci , vol.117 , pp. 5269-5282
    • Delaguillaumie, A.1    Harriague, J.2    Kohanna, S.3    Bismuth, G.4    Rubinstein, E.5    Seigneuret, M.6    Conjeaud, H.7
  • 49
    • 80054096264 scopus 로고    scopus 로고
    • CD63 is an essential cofactor to leukocyte recruitment by endothelial P-selectin
    • Doyle EL, Ridger V, Ferraro F, Turmaine M, Saftig P, Cutler DF (2011) CD63 is an essential cofactor to leukocyte recruitment by endothelial P-selectin. Blood 118:4265-4273
    • (2011) Blood , vol.118 , pp. 4265-4273
    • Doyle, E.L.1    Ridger, V.2    Ferraro, F.3    Turmaine, M.4    Saftig, P.5    Cutler, D.F.6
  • 52
    • 77950540047 scopus 로고    scopus 로고
    • A conserved tetraspanin subfamily promotes Notch signaling in Caenorhabditis elegans and in human cells
    • Dunn CD, Sulis ML, Ferrando AA, Greenwald I (2010) A conserved tetraspanin subfamily promotes Notch signaling in Caenorhabditis elegans and in human cells. Proc Natl Acad Sci USA 107:5907-5912
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 5907-5912
    • Dunn, C.D.1    Sulis, M.L.2    Ferrando, A.A.3    Greenwald, I.4
  • 53
    • 0344875471 scopus 로고    scopus 로고
    • Direct binding of the ligand PSG17 to CD9 requires a CD9 site essential for sperm-egg fusion
    • Ellerman DA, Ha C, Primakoff P, Myles DG, Dveksler GS (2003) Direct binding of the ligand PSG17 to CD9 requires a CD9 site essential for sperm-egg fusion. Mol Biol Cell 14:5098-5103
    • (2003) Mol Biol Cell , vol.14 , pp. 5098-5103
    • Ellerman, D.A.1    Ha, C.2    Primakoff, P.3    Myles, D.G.4    Dveksler, G.S.5
  • 55
    • 0028958669 scopus 로고
    • The CD19/CR2/TAPA-1 complex of B lymphocytes: Linking natural to acquired immunity
    • Fearon DT, Carter RH (1995) The CD19/CR2/TAPA-1 complex of B lymphocytes: linking natural to acquired immunity. Annu Rev Immunol 13:127-149
    • (1995) Annu Rev Immunol , vol.13 , pp. 127-149
    • Fearon, D.T.1    Carter, R.H.2
  • 56
    • 0345803938 scopus 로고    scopus 로고
    • The CD81 tetraspanin facilitates instantaneous leukocyte VLA-4 adhesion strengthening to Vascular Cell Adhesion Molecule 1 (VCAM-1) under shear flow
    • Feigelson SW, Grabovsky V, Shamri R, Levy S, Alon R (2003) The CD81 tetraspanin facilitates instantaneous leukocyte VLA-4 adhesion strengthening to Vascular Cell Adhesion Molecule 1 (VCAM-1) under shear flow. J Biol Chem 278:51203-51212
    • (2003) J Biol Chem , vol.278 , pp. 51203-51212
    • Feigelson, S.W.1    Grabovsky, V.2    Shamri, R.3    Levy, S.4    Alon, R.5
  • 57
    • 0033558218 scopus 로고    scopus 로고
    • Transmembrane 4 superfamily protein CD151 (PETA-3) associates with beta 1 and alpha IIb beta 3 integrins in haemopoietic cell lines and modulates cell-cell adhesion
    • Fitter S, Sincock PM, Jolliffe CN, Ashman LK (1999) Transmembrane 4 superfamily protein CD151 (PETA-3) associates with beta 1 and alpha IIb beta 3 integrins in haemopoietic cell lines and modulates cell-cell adhesion. Biochem J 338:61-70
    • (1999) Biochem J , vol.338 , pp. 61-70
    • Fitter, S.1    Sincock, P.M.2    Jolliffe, C.N.3    Ashman, L.K.4
  • 58
    • 78049511240 scopus 로고    scopus 로고
    • Palmitoylation-dependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes
    • Flannery AR, Czibener C, Andrews NW (2010) Palmitoylation-dependent association with CD63 targets the Ca2+ sensor synaptotagmin VII to lysosomes. J Cell Biol 191:599-613
    • (2010) J Cell Biol , vol.191 , pp. 599-613
    • Flannery, A.R.1    Czibener, C.2    Rews, N.W.3
  • 59
    • 34548422439 scopus 로고    scopus 로고
    • Molecular scaffolds regulate bidirectional crosstalk between Wnt and classical seven-transmembrane-domain receptor signaling pathways
    • Force T, Woulfe K, Koch WJ, Kerkela R (2007) Molecular scaffolds regulate bidirectional crosstalk between Wnt and classical seven-transmembrane-domain receptor signaling pathways. Sci STKE 2007:e41
    • (2007) Sci STKE , vol.2007
    • Force, T.1    Woulfe, K.2    Koch, W.J.3    Kerkela, R.4
  • 62
    • 33846205677 scopus 로고    scopus 로고
    • Role of peripherin/rds in vertebrate photoreceptor architecture and inherited retinal degenerations
    • Goldberg AF (2006) Role of peripherin/rds in vertebrate photoreceptor architecture and inherited retinal degenerations. Int Rev Cytol 253:131-175
    • (2006) Int Rev Cytol , vol.253 , pp. 131-175
    • Goldberg, A.F.1
  • 66
    • 20044367301 scopus 로고    scopus 로고
    • Binding of pregnancy-specific glycoprotein 17 to CD9 on macrophages induces secretion of IL-10, IL-6, PGE2, and TGF-beta1
    • Ha CT, Waterhouse R, Wessells J, Wu JA, Dveksler GS (2005) Binding of pregnancy-specific glycoprotein 17 to CD9 on macrophages induces secretion of IL-10, IL-6, PGE2, and TGF-beta1. J Leukoc Biol 77:948-957
    • (2005) J Leukoc Biol , vol.77 , pp. 948-957
    • Ha, C.T.1    Waterhouse, R.2    Wessells, J.3    Wu, J.A.4    Dveksler, G.S.5
  • 67
    • 84869211737 scopus 로고    scopus 로고
    • The TspanC8 subgroup of tetraspanins interacts with a disintegrin and metalloprotease 10 (ADAM10) and regulates its maturation and cell surface expression
    • Haining EJ, Yang J, Bailey RL, Khan K, Collier R, Tsai S, Watson SP, Frampton J, Garcia P, Tomlinson MG (2012) The TspanC8 subgroup of tetraspanins interacts with a disintegrin and metalloprotease 10 (ADAM10) and regulates its maturation and cell surface expression. J Biol Chem 287:39753-39765
    • (2012) J Biol Chem , vol.287 , pp. 39753-39765
    • Haining, E.J.1    Yang, J.2    Bailey, R.L.3    Khan, K.4    Collier, R.5    Tsai, S.6    Watson, S.P.7    Frampton, J.8    Garcia, P.9    Tomlinson, M.G.10
  • 69
    • 0344708475 scopus 로고    scopus 로고
    • Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain
    • Hemler ME (2003) Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain. Annu Rev Cell Dev Biol 19:397-422
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 397-422
    • Hemler, M.E.1
  • 70
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler ME (2005) Tetraspanin functions and associated microdomains. Nat Rev Mol Cell Biol 6:801-811
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 71
    • 33745238967 scopus 로고    scopus 로고
    • Recombinant extracellular domains of tetraspanin proteins are potent inhibitors of the infection of macrophages by human immunodeficiency virus type 1
    • Ho SH, Martin F, Higginbottom A, Partridge LJ, Parthasarathy V, Moseley GW, Lopez P, Cheng-Mayer C, Monk PN (2006) Recombinant extracellular domains of tetraspanin proteins are potent inhibitors of the infection of macrophages by human immunodeficiency virus type 1. J Virol 80:6487-6496
    • (2006) J Virol , vol.80 , pp. 6487-6496
    • Ho, S.H.1    Martin, F.2    Higginbottom, A.3    Partridge, L.J.4    Parthasarathy, V.5    Moseley, G.W.6    Lopez, P.7    Cheng-Mayer, C.8    Monk, P.N.9
  • 73
    • 28644444179 scopus 로고    scopus 로고
    • The phylogenetic analysis of tetraspanins projects the evolution of cell-cell interactions from unicellular to multicellular organisms
    • Huang S, Yuan S, Dong M, Su J, Yu C, Shen Y, Xie X, Yu Y, Yu X, Chen S, Zhang S, Pontarotti P, Xu A (2005) The phylogenetic analysis of tetraspanins projects the evolution of cell-cell interactions from unicellular to multicellular organisms. Genomics 86:674-684
    • (2005) Genomics , vol.86 , pp. 674-684
    • Huang, S.1    Yuan, S.2    Dong, M.3    Su, J.4    Yu, C.5    Shen, Y.6    Xie, X.7    Yu, Y.8    Yu, X.9    Chen, S.10    Zhang, S.11    Pontarotti, P.12    Xu, A.13
  • 74
    • 0027521558 scopus 로고
    • C33 antigen and M38 antigen recognized by monoclonal antibodies inhibitory to syncytium formation by human T cell leukemia virus type 1 are both members of the transmembrane 4 superfamily and associate with each other and with CD4 or CD8 in T cells
    • Imai T, Yoshie O (1993) C33 antigen and M38 antigen recognized by monoclonal antibodies inhibitory to syncytium formation by human T cell leukemia virus type 1 are both members of the transmembrane 4 superfamily and associate with each other and with CD4 or CD8 in T cells. J Immunol 151:6470-6481
    • (1993) J Immunol , vol.151 , pp. 6470-6481
    • Imai, T.1    Yoshie, O.2
  • 75
    • 0029112968 scopus 로고
    • Molecular analyses of the association of CD4 with two members of the transmembrane 4 superfamily CD81 and CD82
    • Imai T, Kakizaki M, Nishimura M, Yoshie O (1995) Molecular analyses of the association of CD4 with two members of the transmembrane 4 superfamily CD81 and CD82. J Immunol 155:1229-1239
    • (1995) J Immunol , vol.155 , pp. 1229-1239
    • Imai, T.1    Kakizaki, M.2    Nishimura, M.3    Yoshie, O.4
  • 76
    • 0030696936 scopus 로고    scopus 로고
    • Analysis of the tetraspanin CD9-integrin â IIb á3 (GPIIb-IIIa) complex in platelet membranes and transfected cells
    • Indig FE, Diaz-Gonzalez F, Ginsberg MH (1997) Analysis of the tetraspanin CD9-integrin â IIb á3 (GPIIb-IIIa) complex in platelet membranes and transfected cells. Biochem J 327:291-298
    • (1997) Biochem J , vol.327 , pp. 291-298
    • Indig, F.E.1    Diaz-Gonzalez, F.2    Ginsberg, M.H.3
  • 77
    • 0842301340 scopus 로고    scopus 로고
    • Tetraspanin protein CD9 is a novel paranodal component regulating paranodal junctional formation
    • Ishibashi T, Ding L, Ikenaka K, Inoue Y, Miyado K, Mekada E, Baba H (2004) Tetraspanin protein CD9 is a novel paranodal component regulating paranodal junctional formation. J Neurosci 24:96-102
    • (2004) J Neurosci , vol.24 , pp. 96-102
    • Ishibashi, T.1    Ding, L.2    Ikenaka, K.3    Inoue, Y.4    Miyado, K.5    Mekada, E.6    Baba, H.7
  • 78
    • 0034746811 scopus 로고    scopus 로고
    • CD63 associates with the alphaIIb beta3 integrin-CD9 complex on the surface of activated platelets
    • Israels SJ, McMillan-Ward EM, Easton J, Robertson C, McNicol A (2001) CD63 associates with the alphaIIb beta3 integrin-CD9 complex on the surface of activated platelets. Thromb Haemost 85:134-141
    • (2001) Thromb Haemost , vol.85 , pp. 134-141
    • Israels, S.J.1    McMillan-Ward, E.M.2    Easton, J.3    Robertson, C.4    McNicol, A.5
  • 79
    • 0028284810 scopus 로고
    • Heparinbinding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity
    • Iwamoto R, Higashiyama S, Mitamura T, Taniguchi N, Klagsbrun M, Mekada E (1994) Heparinbinding EGF-like growth factor, which acts as the diphtheria toxin receptor, forms a complex with membrane protein DRAP27/CD9, which up-regulates functional receptors and diphtheria toxin sensitivity. EMBO J 13:2322-2330
    • (1994) EMBO J , vol.13 , pp. 2322-2330
    • Iwamoto, R.1    Higashiyama, S.2    Mitamura, T.3    Taniguchi, N.4    Klagsbrun, M.5    Mekada, E.6
  • 80
    • 0026488252 scopus 로고
    • Crystal structure at 2.8 a resolution of a soluble form of the cell adhesion molecule CD2
    • Jones EY, Davis SJ, Williams AF, Harlos K, Stuart DI (1992) Crystal structure at 2.8 a resolution of a soluble form of the cell adhesion molecule CD2. Nature 360:232-239
    • (1992) Nature , vol.360 , pp. 232-239
    • Jones, E.Y.1    Davis, S.J.2    Williams, A.F.3    Harlos, K.4    Stuart, D.I.5
  • 81
    • 0030452494 scopus 로고    scopus 로고
    • Functional significance of CD9 association with á1 integ-rins in human epidermal keratinocytes
    • Jones PH, Bishop LA, Watt FM (1996) Functional significance of CD9 association with á1 integ-rins in human epidermal keratinocytes. Cell Adhes Commun 4:297-305
    • (1996) Cell Adhes Commun , vol.4 , pp. 297-305
    • Jones, P.H.1    Bishop, L.A.2    Watt, F.M.3
  • 82
    • 33748371637 scopus 로고    scopus 로고
    • Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein
    • Jung KK, Liu XW, Chirco R, Fridman R, Kim HR (2006) Identification of CD63 as a tissue inhibitor of metalloproteinase-1 interacting cell surface protein. EMBO J 25:3934-3942
    • (2006) EMBO J , vol.25 , pp. 3934-3942
    • Jung, K.K.1    Liu, X.W.2    Chirco, R.3    Fridman, R.4    Kim, H.R.5
  • 83
    • 70349838225 scopus 로고    scopus 로고
    • TSPAN12 regulates retinal vascular development by promoting Norrin-but not Wnt-induced FZD4/beta-catenin signaling
    • Junge HJ, Yang S, Burton JB, Paes K, Shu X, French DM, Costa M, Rice DS, Ye W (2009) TSPAN12 regulates retinal vascular development by promoting Norrin-but not Wnt-induced FZD4/beta-catenin signaling. Cell 139:299-311
    • (2009) Cell , vol.139 , pp. 299-311
    • Junge, H.J.1    Yang, S.2    Burton, J.B.3    Paes, K.4    Shu, X.5    French, D.M.6    Costa, M.7    Rice, D.S.8    Ye, W.9
  • 85
    • 0036302083 scopus 로고    scopus 로고
    • Infertility of CD9-deficient mouse eggs is reversed by mouse CD9, human CD9, or mouse CD81; polyadenylated mRNA injection developed for molecular analysis of sperm-egg fusion
    • Kaji K, Oda S, Miyazaki S, Kudo A (2002) Infertility of CD9-deficient mouse eggs is reversed by mouse CD9, human CD9, or mouse CD81; polyadenylated mRNA injection developed for molecular analysis of sperm-egg fusion. Dev Biol 247:327-334
    • (2002) Dev Biol , vol.247 , pp. 327-334
    • Kaji, K.1    Oda, S.2    Miyazaki, S.3    Kudo, A.4
  • 86
    • 4944239350 scopus 로고    scopus 로고
    • CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin
    • Karamatic CV, Burton N, Kagan A, Green CA, Levene C, Flinter F, Brady RL, Daniels G, Anstee DJ (2004) CD151, the first member of the tetraspanin (TM4) superfamily detected on erythrocytes, is essential for the correct assembly of human basement membranes in kidney and skin. Blood 104:2217-2223
    • (2004) Blood , vol.104 , pp. 2217-2223
    • Karamatic, C.V.1    Burton, N.2    Kagan, A.3    Green, C.A.4    Levene, C.5    Flinter, F.6    Brady, R.L.7    Daniels, G.8    Anstee, D.J.9
  • 87
    • 0037144837 scopus 로고    scopus 로고
    • An extracellular site on tetraspanin CD151 determines alpha 3 and alpha 6 integrin-dependent cellular morphology
    • Kazarov AR, Yang X, Stipp CS, Sehgal B, Hemler ME (2002) An extracellular site on tetraspanin CD151 determines alpha 3 and alpha 6 integrin-dependent cellular morphology. J Cell Biol 158:1299-1309
    • (2002) J Cell Biol , vol.158 , pp. 1299-1309
    • Kazarov, A.R.1    Yang, X.2    Stipp, C.S.3    Sehgal, B.4    Hemler, M.E.5
  • 91
    • 67649598285 scopus 로고    scopus 로고
    • Demonstration of catch bonds between an integrin and its ligand
    • Kong F, Garcia AJ, Mould AP, Humphries MJ, Zhu C (2009) Demonstration of catch bonds between an integrin and its ligand. J Cell Biol 185:1275-1284
    • (2009) J Cell Biol , vol.185 , pp. 1275-1284
    • Kong, F.1    Garcia, A.J.2    Mould, A.P.3    Humphries, M.J.4    Zhu, C.5
  • 92
    • 0029988151 scopus 로고    scopus 로고
    • A neural tetraspanin, encoded by late bloomer, that facilitates synapse formation
    • Kopczynski CC, Davis GW, Goodman CS (1996) A neural tetraspanin, encoded by late bloomer, that facilitates synapse formation. Science 271:1867-1870
    • (1996) Science , vol.271 , pp. 1867-1870
    • Kopczynski, C.C.1    Davis, G.W.2    Goodman, C.S.3
  • 93
    • 36749037222 scopus 로고    scopus 로고
    • A novel cysteine cross-linking method reveals a direct association between claudin-1 and tetraspanin CD9
    • Kovalenko OV, Yang XH, Hemler ME (2007) A novel cysteine cross-linking method reveals a direct association between claudin-1 and tetraspanin CD9. Mol Cell Proteomics 6:1855-1867
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1855-1867
    • Kovalenko, O.V.1    Yang, X.H.2    Hemler, M.E.3
  • 95
    • 65249142254 scopus 로고    scopus 로고
    • Tetraspanin proteins regulate membrane type-1 matrix metalloproteinase-dependent pericellular proteolysis
    • Lafleur MA, Xu D, Hemler ME (2009) Tetraspanin proteins regulate membrane type-1 matrix metalloproteinase-dependent pericellular proteolysis. Mol Biol Cell 20:2030-2040
    • (2009) Mol Biol Cell , vol.20 , pp. 2030-2040
    • Lafleur, M.A.1    Xu, D.2    Hemler, M.E.3
  • 96
    • 0031573837 scopus 로고    scopus 로고
    • Functional analysis of four tetraspans, CD9, CD53, CD81, and CD82, suggests a common role in costimulation, cell adhesion, and migration: Only CD9 upregulates HB-EGF activity
    • Lagaudriere-Gesbert C, Le Naour F, Lebel-Binay S, Billard M, Lemichez E, Boucheix C, Conjeaud H, Rubinstein E (1997a) Functional analysis of four tetraspans, CD9, CD53, CD81, and CD82, suggests a common role in costimulation, cell adhesion, and migration: only CD9 upregulates HB-EGF activity. Cell Immunol 182:105-112
    • (1997) Cell Immunol , vol.182 , pp. 105-112
    • Lagaudriere-Gesbert, C.1    Le Naour, F.2    Lebel-Binay, S.3    Billard, M.4    Lemichez, E.5    Boucheix, C.6    Conjeaud, H.7    Rubinstein, E.8
  • 97
    • 0031569284 scopus 로고    scopus 로고
    • The tetraspanin protein CD82 associates with both free HLA class I heavy chain and heterodimeric beta2-microglobulin complexes
    • Lagaudriere-Gesbert C, Lebel-Binay S, Wiertz E, Ploegh HL, Fradelizi D, Conjeaud H (1997b) The tetraspanin protein CD82 associates with both free HLA class I heavy chain and heterodimeric beta2-microglobulin complexes. J Immunol 158:2790-2797
    • (1997) J Immunol , vol.158 , pp. 2790-2797
    • Lagaudriere-Gesbert, C.1    Lebel-Binay, S.2    Wiertz, E.3    Ploegh, H.L.4    Fradelizi, D.5    Conjeaud, H.6
  • 98
    • 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, Lebel-Binay S, Hubeau C, Fradelizi D, Conjeaud H (1998) Signaling through the tetraspanin CD82 triggers its association with the cytoskeleton leading to sustained morphological changes and T cell activation. Eur J Immunol 28:4332-4344
    • (1998) Eur J Immunol , vol.28 , pp. 4332-4344
    • Lagaudriere-Gesbert, C.1    Lebel-Binay, S.2    Hubeau, C.3    Fradelizi, D.4    Conjeaud, H.5
  • 100
    • 33749635768 scopus 로고    scopus 로고
    • Syntenin-1 is a new component of tetraspanin-enriched microdomains: Mechanisms and consequences of the interaction of syntenin-1 with CD63
    • Latysheva N, Muratov G, Rajesh S, Padgett M, Hotchin NA, Overduin M, Berditchevski F (2006) Syntenin-1 is a new component of tetraspanin-enriched microdomains: mechanisms and consequences of the interaction of syntenin-1 with CD63. Mol Cell Biol 26:7707-7718
    • (2006) Mol Cell Biol , vol.26 , pp. 7707-7718
    • Latysheva, N.1    Muratov, G.2    Rajesh, S.3    Padgett, M.4    Hotchin, N.A.5    Overduin, M.6    Berditchevski, F.7
  • 101
    • 4944252716 scopus 로고    scopus 로고
    • The tetraspanin superfamily member CD151 regulates outside-in integrin alphaIIbbeta3 signaling and platelet function
    • Lau LM, Wee JL, Wright MD, Moseley GW, Hogarth PM, Ashman LK, Jackson DE (2004) The tetraspanin superfamily member CD151 regulates outside-in integrin alphaIIbbeta3 signaling and platelet function. Blood 104:2368-2375
    • (2004) Blood , vol.104 , pp. 2368-2375
    • Lau, L.M.1    Wee, J.L.2    Wright, M.D.3    Moseley, G.W.4    Hogarth, P.M.5    Ashman, L.K.6    Jackson, D.E.7
  • 104
    • 0029055433 scopus 로고
    • CD82, member of the tetra-span-transmembrane protein family, is a costimulatory protein for T cell activation
    • Lebel-Binay S, Lagaudriere C, Fradelizi D, Conjeaud H (1995) CD82, member of the tetra-span-transmembrane protein family, is a costimulatory protein for T cell activation. J Immunol 155:101-110
    • (1995) J Immunol , vol.155 , pp. 101-110
    • Lebel-Binay, S.1    Lagaudriere, C.2    Fradelizi, D.3    Conjeaud, H.4
  • 105
    • 42149159461 scopus 로고    scopus 로고
    • The tumour-associated antigen L6 (L6-Ag) is recruited to the tetraspanin-enriched microdomains: Implication for tumour cell motility
    • Lekishvili T, Fromm E, Mujoomdar M, Berditchevski F (2008) The tumour-associated antigen L6 (L6-Ag) is recruited to the tetraspanin-enriched microdomains: implication for tumour cell motility. J Cell Sci 121:685-694
    • (2008) J Cell Sci , vol.121 , pp. 685-694
    • Lekishvili, T.1    Fromm, E.2    Mujoomdar, M.3    Berditchevski, F.4
  • 106
    • 13444259476 scopus 로고    scopus 로고
    • The tetraspanin web modulates immune-signalling complexes
    • Levy S, Shoham T (2005) The tetraspanin web modulates immune-signalling complexes. Nat Rev Immunol 5:136-148
    • (2005) Nat Rev Immunol , vol.5 , pp. 136-148
    • Levy, S.1    Shoham, T.2
  • 107
  • 108
    • 57649121585 scopus 로고    scopus 로고
    • The single subunit transmembrane E3 ligase Gene Related to Anergy In Lymphocytes (GRAIL) captures and then ubiquitinates transmembrane proteins across the cell membrane
    • Lineberry N, Su L, Soares L, Fathman CG (2008) The single subunit transmembrane E3 ligase Gene Related to Anergy In Lymphocytes (GRAIL) captures and then ubiquitinates transmembrane proteins across the cell membrane. J Biol Chem 283:28497-28505
    • (2008) J Biol Chem , vol.283 , pp. 28497-28505
    • Lineberry, N.1    Su, L.2    Soares, L.3    Fathman, C.G.4
  • 109
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D, Simons K (2010) Lipid rafts as a membrane-organizing principle. Science 327:46-50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 110
    • 2342653563 scopus 로고    scopus 로고
    • Dynamic regulation of a GPCR-tetraspanin-G protein complex on intact cells: Central role of CD81 in facilitating GPR56-Galpha q/11 association
    • Little KD, Hemler ME, Stipp CS (2004) Dynamic regulation of a GPCR-tetraspanin-G protein complex on intact cells: central role of CD81 in facilitating GPR56-Galpha q/11 association. Mol Biol Cel! 15:2375-2387
    • (2004) Mol Biol Cell , vol.15 , pp. 2375-2387
    • Little, K.D.1    Hemler, M.E.2    Stipp, C.S.3
  • 111
    • 0033153759 scopus 로고    scopus 로고
    • A CD9, IIb3, integrin-associated protein, and GPIb/V/IX complex on the surface of human platelets is influenced by IIb3 conformational states
    • Longhurst CM, White MM, Wilkinson DA, Jennings LK (1999) A CD9, IIb3, integrin-associated protein, and GPIb/V/IX complex on the surface of human platelets is influenced by IIb3 conformational states. Eur J Biochem 263:104-111
    • (1999) Eur J Biochem , vol.263 , pp. 104-111
    • Longhurst, C.M.1    White, M.M.2    Wilkinson, D.A.3    Jennings, L.K.4
  • 113
    • 65449166493 scopus 로고    scopus 로고
    • CD9 negatively regulates integrin alpha(Llb)beta(3) activation and could thus prevent excessive platelet recruitment at sites of vascular injury
    • Mangin PH, Kleitz L, Boucheix C, Gachet C, Lanza F (2009) CD9 negatively regulates integrin alpha(llb)beta(3) activation and could thus prevent excessive platelet recruitment at sites of vascular injury. J Thromb Haemost 7:900-902
    • (2009) J Thromb Haemost , vol.7 , pp. 900-902
    • Mangin, P.H.1    Kleitz, L.2    Boucheix, C.3    Gachet, C.4    Lanza, F.5
  • 114
    • 0030239653 scopus 로고    scopus 로고
    • Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29)
    • Mannion BA, Berditchevski F, Kraeft SK, Chen LB, Hemler ME (1996) Transmembrane-4 superfamily proteins CD81 (TAPA-1), CD82, CD63, and CD53 specifically associated with integrin alpha 4 beta 1 (CD49d/CD29). J Immunol 157:2039-2047
    • (1996) J Immunol , vol.157 , pp. 2039-2047
    • Mannion, B.A.1    Berditchevski, F.2    Kraeft, S.K.3    Chen, L.B.4    Hemler, M.E.5
  • 115
    • 79952206848 scopus 로고    scopus 로고
    • The role of Syk/CARD9-coupled C-type lectin receptors in immunity to Mycobacterium tuberculosis infections
    • Marakalala MJ, Graham LM, Brown GD (2010) The role of Syk/CARD9-coupled C-type lectin receptors in immunity to Mycobacterium tuberculosis infections. Clin Dev Immunol 2010:567-571
    • (2010) Clin Dev Immunol , vol.2010 , pp. 567-571
    • Marakalala, M.J.1    Graham, L.M.2    Brown, G.D.3
  • 116
    • 45449105164 scopus 로고    scopus 로고
    • Protein modulation of lipids, and vice-versa, in membranes
    • Marsh D (2008) Protein modulation of lipids, and vice-versa, in membranes. Biochim Biophys Acta 1778:1545-1575
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1545-1575
    • Marsh, D.1
  • 119
    • 0035869540 scopus 로고    scopus 로고
    • CD36 associates with CD9 and integrins on human blood platelets
    • Miao WM, Vasile E, Lane WS, Lawler J (2001) CD36 associates with CD9 and integrins on human blood platelets. Blood 97:1689-1696
    • (2001) Blood , vol.97 , pp. 1689-1696
    • Miao, W.M.1    Vasile, E.2    Lane, W.S.3    Lawler, J.4
  • 120
    • 33745235141 scopus 로고    scopus 로고
    • Structural basis for tetraspanin functions as revealed by the cryo-EM structure of uroplakin complexes at 6-A resolution
    • Min G, Wang H, Sun TT, Kong XP (2006) Structural basis for tetraspanin functions as revealed by the cryo-EM structure of uroplakin complexes at 6-A resolution. J Cell Biol 173:975-983
    • (2006) J Cell Biol , vol.173 , pp. 975-983
    • Min, G.1    Wang, H.2    Sun, T.T.3    Kong, X.P.4
  • 121
    • 0037114132 scopus 로고    scopus 로고
    • Cutting edge: Dynamic redistribution of tetraspanin CD81 at the central zone of the immune synapse in both T lymphocytes and APC
    • Mittelbrunn M, Yanez-Mo M, Sancho D, Ursa A, Sanchez-Madrid F (2002) Cutting edge: dynamic redistribution of tetraspanin CD81 at the central zone of the immune synapse in both T lymphocytes and APC. J Immunol 169:6691-6695
    • (2002) J Immunol , vol.169 , pp. 6691-6695
    • Mittelbrunn, M.1    Yanez-Mo, M.2    Sancho, D.3    Ursa, A.4    Sanchez-Madrid, F.5
  • 124
    • 9444231148 scopus 로고    scopus 로고
    • Tetraspanin protein (TSP-15) is required for epidermal integrity in Caenorhabditis elegans
    • Moribe H, Yochem J, Yamada H, Tabuse Y, Fujimoto T, Mekada E (2004) Tetraspanin protein (TSP-15) is required for epidermal integrity in Caenorhabditis elegans. J Cell Sci 117:5209-5220
    • (2004) J Cell Sci , vol.117 , pp. 5209-5220
    • Moribe, H.1    Yochem, J.2    Yamada, H.3    Tabuse, Y.4    Fujimoto, T.5    Mekada, E.6
  • 126
    • 0034674432 scopus 로고    scopus 로고
    • Importance of the major extracellular domain of CD9 and the Epidermal Growth Factor (EGF)-like domain of heparin-binding EGF-like growth factor for Up-regulation of binding and activity
    • Nakamura K, Mitamura T, Takahashi T, Kobayashi T, Mekada E (2000) Importance of the major extracellular domain of CD9 and the Epidermal Growth Factor (EGF)-like domain of heparin-binding EGF-like growth factor for Up-regulation of binding and activity. J Biol Chem 275:18284-18290
    • (2000) J Biol Chem , vol.275 , pp. 18284-18290
    • Nakamura, K.1    Mitamura, T.2    Takahashi, T.3    Kobayashi, T.4    Mekada, E.5
  • 127
    • 0031739195 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase, an ecto-enzyme regulator of intracellular redox potential, is a component of TM4 signal transduction complexes
    • Nichols TC, Guthridge JM, Karp DR, Molina H, Fletcher DR, Holers VM (1998) Gamma-glutamyl transpeptidase, an ecto-enzyme regulator of intracellular redox potential, is a component of TM4 signal transduction complexes. Eur J Immunol 28:4123-4129
    • (1998) Eur J Immunol , vol.28 , pp. 4123-4129
    • Nichols, T.C.1    Guthridge, J.M.2    Karp, D.R.3    Molina, H.4    Fletcher, D.R.5    Holers, V.M.6
  • 130
    • 77953158444 scopus 로고    scopus 로고
    • Tetraspanin CD151 regulates growth of mammary epithelial cells in three-dimensional extracellular matrix: Implication for mammary ductal carcinoma in situ
    • Novitskaya V, Romanska H, Dawoud M, Jones JL, Berditchevski F (2010) Tetraspanin CD151 regulates growth of mammary epithelial cells in three-dimensional extracellular matrix: implication for mammary ductal carcinoma in situ. Cancer Res 70:4698-4708
    • (2010) Cancer Res , vol.70 , pp. 4698-4708
    • Novitskaya, V.1    Romanska, H.2    Dawoud, M.3    Jones, J.L.4    Berditchevski, F.5
  • 131
    • 0034710619 scopus 로고    scopus 로고
    • Attenuation of EGF receptor signaling by a metastasis suppressor, the tetraspanin CD82/KAI-1
    • Odintsova E, Sugiura T, Berditchevski F (2000) Attenuation of EGF receptor signaling by a metastasis suppressor, the tetraspanin CD82/KAI-1. Curr Biol 10:1009-1012
    • (2000) Curr Biol , vol.10 , pp. 1009-1012
    • Odintsova, E.1    Sugiura, T.2    Berditchevski, F.3
  • 132
    • 0344897638 scopus 로고    scopus 로고
    • Tetraspanin CD82 regulates compart-mentalisation and ligand-induced dimerization of EGFR
    • Odintsova E, Voortman J, Gilbert E, Berditchevski F (2003) Tetraspanin CD82 regulates compart-mentalisation and ligand-induced dimerization of EGFR. J Cell Sci 116:4557-4566
    • (2003) J Cell Sci , vol.116 , pp. 4557-4566
    • Odintsova, E.1    Voortman, J.2    Gilbert, E.3    Berditchevski, F.4
  • 134
    • 0141996367 scopus 로고    scopus 로고
    • The ekeko mutant demonstrates a role for tetraspanin-like protein in plant development
    • Olmos E, Reiss B, Dekker K (2003) The ekeko mutant demonstrates a role for tetraspanin-like protein in plant development. Biochem Biophys Res Commun 310:1054-1061
    • (2003) Biochem Biophys Res Commun , vol.310 , pp. 1054-1061
    • Olmos, E.1    Reiss, B.2    Dekker, K.3
  • 135
    • 0035967503 scopus 로고    scopus 로고
    • GM3 ganglioside inhibits CD9-facilitated haptotactic cell motility: Coexpression of GM3 and CD9 is essential in the downregulation of tumor cell motility and malignancy
    • Ono M, Handa K, Sonnino S, Withers DA, Nagai H, Hakomori S (2001) GM3 ganglioside inhibits CD9-facilitated haptotactic cell motility: coexpression of GM3 and CD9 is essential in the downregulation of tumor cell motility and malignancy. Biochemistry 40:6414-6421
    • (2001) Biochemistry , vol.40 , pp. 6414-6421
    • Ono, M.1    Handa, K.2    Sonnino, S.3    Withers, D.A.4    Nagai, H.5    Hakomori, S.6
  • 137
    • 33846900177 scopus 로고    scopus 로고
    • The developmental regulation of CD81 in the rat retina
    • Pan Y, Brown C, Wang X, Geisert EE (2007) The developmental regulation of CD81 in the rat retina. Mol Vis 13:181-189
    • (2007) Mol Vis , vol.13 , pp. 181-189
    • Pan, Y.1    Brown, C.2    Wang, X.3    Geisert, E.E.4
  • 142
  • 144
    • 77954210220 scopus 로고    scopus 로고
    • An updated overview on Wnt signaling pathways: A prelude for more
    • Rao TP, Kuhl M (2010) An updated overview on Wnt signaling pathways: a prelude for more. Circ Res 106:1798-1806
    • (2010) Circ Res , vol.106 , pp. 1798-1806
    • Rao, T.P.1    Kuhl, M.2
  • 145
    • 63649141727 scopus 로고    scopus 로고
    • The “A Disintegrin And Metalloprotease” (ADAM) family of sheddases: Physiological and cellular functions
    • Reiss K, Saftig P (2009) The “A Disintegrin And Metalloprotease” (ADAM) family of sheddases: physiological and cellular functions. Semin Cell Dev Biol 20:126-137
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 126-137
    • Reiss, K.1    Saftig, P.2
  • 146
    • 78650023067 scopus 로고    scopus 로고
    • Tetraspanins in human epithelial malignancies
    • Romanska HM, Berditchevski F (2011) Tetraspanins in human epithelial malignancies. J Pathol 223:4-14
    • (2011) J Pathol , vol.223 , pp. 4-14
    • Romanska, H.M.1    Berditchevski, F.2
  • 148
    • 10244261559 scopus 로고    scopus 로고
    • CD9, CD63, CD81 and CD82 are components of a surface tetraspan network connected to HLA-DR and VLA integrins
    • Rubinstein E, Le Naour F, Lagaudriere C, Billard M, Conjeaud H, Boucheix C (1996) CD9, CD63, CD81 and CD82 are components of a surface tetraspan network connected to HLA-DR and VLA integrins. Eur J Immunol 26:2657-2665
    • (1996) Eur J Immunol , vol.26 , pp. 2657-2665
    • Rubinstein, E.1    Le Naour, F.2    Lagaudriere, C.3    Billard, M.4    Conjeaud, H.5    Boucheix, C.6
  • 152
  • 153
    • 33745837412 scopus 로고    scopus 로고
    • EWI-2 and EWI-F link the tetraspanin web to the actin cytoskeleton through their direct association with ezrin-radixin-moesin proteins
    • Sala-Valdes M, Ursa A, Charrin S, Rubinstein E, Hemler ME, Sanchez-Madrid F, Yanez-Mo M (2006) EWI-2 and EWI-F link the tetraspanin web to the actin cytoskeleton through their direct association with ezrin-radixin-moesin proteins. J Biol Chem 281:19665-19675
    • (2006) J Biol Chem , vol.281 , pp. 19665-19675
    • Sala-Valdes, M.1    Ursa, A.2    Charrin, S.3    Rubinstein, E.4    Hemler, M.E.5    Sanchez-Madrid, F.6    Yanez-Mo, M.7
  • 154
    • 0027440436 scopus 로고
    • The TAPA-1 molecule is associated on the surface of B cells with HLA-DR molecules
    • Schick MR, Levy S (1993) The TAPA-1 molecule is associated on the surface of B cells with HLA-DR molecules. J Immunol 151:4090-4097
    • (1993) J Immunol , vol.151 , pp. 4090-4097
    • Schick, M.R.1    Levy, S.2
  • 155
    • 0030021514 scopus 로고    scopus 로고
    • CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the alpha 6/beta 1 integrin and the neural adhesion molecule L1
    • Schmidt C, Kunemund V, Wintergerst ES, Schmitz B, Schachner M (1996) CD9 of mouse brain is implicated in neurite outgrowth and cell migration in vitro and is associated with the alpha 6/beta 1 integrin and the neural adhesion molecule L1. J Neurosci Res 43:12-31
    • (1996) J Neurosci Res , vol.43 , pp. 12-31
    • Schmidt, C.1    Kunemund, V.2    Wintergerst, E.S.3    Schmitz, B.4    Schachner, M.5
  • 156
    • 0024245704 scopus 로고
    • The functional glycoprotein CD9 is variably acylated: Localization of the variably acylated region to a membrane-associated peptide containing the binding site for the agonistic monoclonal antibody 50H.19
    • Seehafer JG, Shou Ching T, Slupsky JR, Shaw ARE (1988) The functional glycoprotein CD9 is variably acylated: localization of the variably acylated region to a membrane-associated peptide containing the binding site for the agonistic monoclonal antibody 50H.19. Biochim Biophys Acta 957:399-410
    • (1988) Biochim Biophys Acta , vol.957 , pp. 399-410
    • Seehafer, J.G.1    Shou Ching, T.2    Slupsky, J.R.3    Shaw, A.4
  • 157
    • 33644820905 scopus 로고    scopus 로고
    • Complete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitis C virus receptor CD81: Conserved and variable structural domains in the tetraspanin superfamily
    • Seigneuret M (2006) Complete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitis C virus receptor CD81: conserved and variable structural domains in the tetraspanin superfamily. Biophys J 90:212-227
    • (2006) Biophys J , vol.90 , pp. 212-227
    • Seigneuret, M.1
  • 158
    • 0033563224 scopus 로고    scopus 로고
    • Selective Tetraspan/integrin complexes (CD81/a4á1, CD151/a3á1, CD151/a6á1) under conditions disrupting tetraspan interactions
    • Serru V, Le Naour F, Billard M, Azorsa DO, Lanza F, Boucheix C, Rubinstein E (1999) Selective Tetraspan/integrin complexes (CD81/a4á1, CD151/a3á1, CD151/a6á1) under conditions disrupting tetraspan interactions. Biochem J 340:103-111
    • (1999) Biochem J , vol.340 , pp. 103-111
    • Serru, V.1    Le Naour, F.2    Billard, M.3    Azorsa, D.O.4    Lanza, F.5    Boucheix, C.6    Rubinstein, E.7
  • 159
    • 51049123096 scopus 로고    scopus 로고
    • DHHC2 affects palmitoylation, stability, and functions of tetraspanins CD9 and CD151
    • Sharma C, Yang XH, Hemler ME (2008) DHHC2 affects palmitoylation, stability, and functions of tetraspanins CD9 and CD151. Mol Biol Cell 19:3415-3425
    • (2008) Mol Biol Cell , vol.19 , pp. 3415-3425
    • Sharma, C.1    Yang, X.H.2    Hemler, M.E.3
  • 161
    • 0034614938 scopus 로고    scopus 로고
    • The tetraspanin CD9 associates with transmembrane TGF-alpha and regulates TGF-alpha-induced EGF receptor activation and cell proliferation
    • Shi W, Fan H, Shum L, Derynck R (2000) The tetraspanin CD9 associates with transmembrane TGF-alpha and regulates TGF-alpha-induced EGF receptor activation and cell proliferation. J Cell Biol 148:591-602
    • (2000) J Cell Biol , vol.148 , pp. 591-602
    • Shi, W.1    Fan, H.2    Shum, L.3    Derynck, R.4
  • 162
    • 0032709802 scopus 로고    scopus 로고
    • Overexpression of CD82 on human T cells enhances LFA-1/ICAM-1-mediated cell-cell adhesion: Functional association between CD82 and LFA-1 in T cell activation
    • Shibagaki N, Hanada K, Yamashita H, Shimada S, Hamada H (1999) Overexpression of CD82 on human T cells enhances LFA-1/ICAM-1-mediated cell-cell adhesion: functional association between CD82 and LFA-1 in T cell activation. Eur J Immunol 29:4081-4091
    • (1999) Eur J Immunol , vol.29 , pp. 4081-4091
    • Shibagaki, N.1    Hanada, K.2    Yamashita, H.3    Shimada, S.4    Hamada, H.5
  • 163
    • 0142059952 scopus 로고    scopus 로고
    • CD151 regulates epithelial cell-cell adhesion through PKC-and Cdc42-dependent actin cytoskeletal reorganization
    • Shigeta M, Sanzen N, Ozawa M, Gu J, Hasegawa H, Sekiguchi K (2003) CD151 regulates epithelial cell-cell adhesion through PKC-and Cdc42-dependent actin cytoskeletal reorganization. J Cell Biol 163:165-176
    • (2003) J Cell Biol , vol.163 , pp. 165-176
    • Shigeta, M.1    Sanzen, N.2    Ozawa, M.3    Gu, J.4    Hasegawa, H.5    Sekiguchi, K.6
  • 165
    • 0141923758 scopus 로고    scopus 로고
    • The tet-raspanin CD81 regulates the expression of CD19 during B cell development in a postendoplasmic reticulum compartment
    • Shoham T, Rajapaksa R, Boucheix C, Rubinstein E, Poe JC, Tedder TF, Levy S (2003) The tet-raspanin CD81 regulates the expression of CD19 during B cell development in a postendoplasmic reticulum compartment. J Immunol 171:4062-4072
    • (2003) J Immunol , vol.171 , pp. 4062-4072
    • Shoham, T.1    Rajapaksa, R.2    Boucheix, C.3    Rubinstein, E.4    Poe, J.C.5    Tedder, T.F.6    Levy, S.7
  • 166
    • 32044459101 scopus 로고    scopus 로고
    • Building of the tetraspanin web: Distinct structural domains of CD81 function in different cellular compartments
    • Shoham T, Rajapaksa R, Kuo CC, Haimovich J, Levy S (2006) Building of the tetraspanin web: distinct structural domains of CD81 function in different cellular compartments. Mol Cell Biol 26:1373-1385
    • (2006) Mol Cell Biol , vol.26 , pp. 1373-1385
    • Shoham, T.1    Rajapaksa, R.2    Kuo, C.C.3    Haimovich, J.4    Levy, S.5
  • 168
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D (2000) Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1:31-39
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 169
    • 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 PM, Fitter S, Parton RG, Berndt MC, Gamble JR, Ashman LK (1999) 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 112:833-844
    • (1999) J Cell Sci , vol.112 , pp. 833-844
    • Sincock, P.M.1    Fitter, S.2    Parton, R.G.3    Berndt, M.C.4    Gamble, J.R.5    Ashman, L.K.6
  • 170
    • 0030587912 scopus 로고    scopus 로고
    • CD63 associates with tyorsine kinase activity and CD11/CD18; and transmits an activation signal in neutrophils
    • Skubitz KM, Campbell KD, Iida J, Skubitz APN (1996) CD63 associates with tyorsine kinase activity and CD11/CD18; and transmits an activation signal in neutrophils. J Immunol 157:3617-3626
    • (1996) J Immunol , vol.157 , pp. 3617-3626
    • Skubitz, K.M.1    Campbell, K.D.2    Iida, J.3    Skubitz, A.4
  • 171
    • 0024349131 scopus 로고
    • Evidence that monoclonal antibodies against CD9 antigen induce specific association between CD9 and the platelet glycoprotein Ilb-IIIa complex
    • Slupsky JR, Seehafer JG, Tang SC, Masellis-Smith A, Shaw AR (1989) Evidence that monoclonal antibodies against CD9 antigen induce specific association between CD9 and the platelet glycoprotein Ilb-IIIa complex. J Biol Chem 264:12289-12293
    • (1989) J Biol Chem , vol.264 , pp. 12289-12293
    • Slupsky, J.R.1    Seehafer, J.G.2    Tang, S.C.3    Masellis-Smith, A.4    Shaw, A.R.5
  • 172
    • 0031058589 scopus 로고    scopus 로고
    • The platelet antigens CD9, CD42 and integrin alpha IIb beta IIIa can be topographically associated and transduce functionally similar signals
    • Slupsky JR, Kamiguti AS, Rhodes NP, Cawley JC, Shaw AR, Zuzel M (1997) The platelet antigens CD9, CD42 and integrin alpha IIb beta IIIa can be topographically associated and transduce functionally similar signals. Eur J Biochem 244:168-175
    • (1997) Eur J Biochem , vol.244 , pp. 168-175
    • Slupsky, J.R.1    Kamiguti, A.S.2    Rhodes, N.P.3    Cawley, J.C.4    Shaw, A.R.5    Zuzel, M.6
  • 173
    • 33646148495 scopus 로고    scopus 로고
    • Tetraspanin KAI1/CD82 suppresses invasion by inhibiting integrin-dependent crosstalk with c-Met receptor and Src kinases
    • Sridhar SC, Miranti CK (2006) Tetraspanin KAI1/CD82 suppresses invasion by inhibiting integrin-dependent crosstalk with c-Met receptor and Src kinases. Oncogene 25:2367-2378
    • (2006) Oncogene , vol.25 , pp. 2367-2378
    • Sridhar, S.C.1    Miranti, C.K.2
  • 174
    • 0034658462 scopus 로고    scopus 로고
    • The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes
    • Sterk LM, Geuijen CA, Oomen LC, Calafat J, Janssen H, Sonnenberg A (2000) The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin alpha6beta4 and may regulate the spatial organization of hemidesmosomes. J Cell Biol 149:969-982
    • (2000) J Cell Biol , vol.149 , pp. 969-982
    • Sterk, L.M.1    Geuijen, C.A.2    Oomen, L.C.3    Calafat, J.4    Janssen, H.5    Sonnenberg, A.6
  • 175
    • 0037087710 scopus 로고    scopus 로고
    • Association of the tetraspanin CD151 with the laminin-binding integrins alpha3beta1, alpha-6beta1, alpha6beta4 and alpha7beta1 in cells in culture and in vivo
    • Sterk LM, Geuijen CA, van den Berg JG, Claessen N, Weening JJ, Sonnenberg A (2002) Association of the tetraspanin CD151 with the laminin-binding integrins alpha3beta1, alpha-6beta1, alpha6beta4 and alpha7beta1 in cells in culture and in vivo. J Cell Sci 115:1161-1173
    • (2002) J Cell Sci , vol.115 , pp. 1161-1173
    • Sterk, L.M.1    Geuijen, C.A.2    Van Den Berg, J.G.3    Claessen, N.4    Weening, J.J.5    Sonnenberg, A.6
  • 176
    • 0035798537 scopus 로고    scopus 로고
    • EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
    • Stipp CS, Kolesnikova TV, Hemler ME (2001a) EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily. J Biol Chem 276:40545-40554
    • (2001) J Biol Chem , vol.276 , pp. 40545-40554
    • Stipp, C.S.1    Kolesnikova, T.V.2    Hemler, M.E.3
  • 177
    • 0035895876 scopus 로고    scopus 로고
    • FPRP, a major, highly stoichiometric, highly specific CD81-and CD9-associated protein
    • Stipp CS, Orlicky D, Hemler ME (2001b) FPRP, a major, highly stoichiometric, highly specific CD81-and CD9-associated protein. J Biol Chem 276:4853-4862
    • (2001) J Biol Chem , vol.276 , pp. 4853-4862
    • Stipp, C.S.1    Orlicky, D.2    Hemler, M.E.3
  • 178
    • 0346849708 scopus 로고    scopus 로고
    • EWI-2 regulates alpha3beta1 integrin-dependent cell functions on laminin-5
    • Stipp CS, Kolesnikova TV, Hemler ME (2003) EWI-2 regulates alpha3beta1 integrin-dependent cell functions on laminin-5. J Cell Biol 163:1167-1177
    • (2003) J Cell Biol , vol.163 , pp. 1167-1177
    • Stipp, C.S.1    Kolesnikova, T.V.2    Hemler, M.E.3
  • 179
    • 33745352577 scopus 로고    scopus 로고
    • Altered phenotype of cultured urothelial and other stratified epithelial cells: Implications for wound healing
    • Sun TT (2006) Altered phenotype of cultured urothelial and other stratified epithelial cells: implications for wound healing. Am J Physiol Renal Physiol 291:F9-F21
    • (2006) Am J Physiol Renal Physiol , vol.291 , pp. FF9-F21
    • Sun, T.T.1
  • 180
    • 0030267031 scopus 로고    scopus 로고
    • Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY
    • Szöllósi J, Horejsí V, Bene L, Angelisová P, Damjanovich S (1996) Supramolecular complexes of MHC class I, MHC class II, CD20, and tetraspan molecules (CD53, CD81, and CD82) at the surface of a B cell line JY. J Immunol 157:2939-2946
    • (1996) J Immunol , vol.157 , pp. 2939-2946
    • Szöllósi, J.1    Horejsí, V.2    Bene, L.3    Angelisová, P.4    Damjanovich, S.5
  • 181
    • 0030690101 scopus 로고    scopus 로고
    • NAG-2 a novel Transmembrane-4 Superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins
    • Tachibana I, Bodorova J, Berditchevski F, Zutter MM, Hemler ME (1997) NAG-2 a novel Transmembrane-4 Superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins. J Biol Chem 272:29181-29189
    • (1997) J Biol Chem , vol.272 , pp. 29181-29189
    • Tachibana, I.1    Bodorova, J.2    Berditchevski, F.3    Zutter, M.M.4    Hemler, M.E.5
  • 183
    • 0025084911 scopus 로고
    • TAPA-1, the target of an antiproliferative antibody, is associated on the cell surface with the Leu-13 antigen
    • Takahashi S, Doss C, Levy S, Levy R (1990) TAPA-1, the target of an antiproliferative antibody, is associated on the cell surface with the Leu-13 antigen. J Immunol 145:2207-2213
    • (1990) J Immunol , vol.145 , pp. 2207-2213
    • Takahashi, S.1    Doss, C.2    Levy, S.3    Levy, R.4
  • 184
    • 34648831077 scopus 로고    scopus 로고
    • Regulation of c-Met signaling by the tetraspanin KAI-1/CD82 affects cancer cell migration
    • Takahashi M, Sugiura T, Abe M, Ishii K, Shirasuna K (2007) Regulation of c-Met signaling by the tetraspanin KAI-1/CD82 affects cancer cell migration. Int J Cancer 121:1919-1929
    • (2007) Int J Cancer , vol.121 , pp. 1919-1929
    • Takahashi, M.1    Sugiura, T.2    Abe, M.3    Ishii, K.4    Shirasuna, K.5
  • 188
    • 0037466459 scopus 로고    scopus 로고
    • Tetraspanin CD63 promotes targeting and lysosomal proteolysis of membrane-type 1 matrix metalloproteinase
    • Takino T, Miyamori H, Kawaguchi N, Uekita T, Seiki M, Sato H (2003) Tetraspanin CD63 promotes targeting and lysosomal proteolysis of membrane-type 1 matrix metalloproteinase. Biochem Biophys Res Commun 304:160-166
    • (2003) Biochem Biophys Res Commun , vol.304 , pp. 160-166
    • Takino, T.1    Miyamori, H.2    Kawaguchi, N.3    Uekita, T.4    Seiki, M.5    Sato, H.6
  • 189
    • 0036291471 scopus 로고    scopus 로고
    • The absence of Tssc6, a member of the tetraspanin superfamily, does not affect lymphoid development but enhances in vitro T-cell proliferative responses
    • Tarrant JM, Groom J, Metcalf D, Li R, Borobokas B, Wright MD, Tarlinton D, Robb L (2002) The absence of Tssc6, a member of the tetraspanin superfamily, does not affect lymphoid development but enhances in vitro T-cell proliferative responses. Mol Cell Biol 22:5006-5018
    • (2002) Mol Cell Biol , vol.22 , pp. 5006-5018
    • Tarrant, J.M.1    Groom, J.2    Metcalf, D.3    Li, R.4    Borobokas, B.5    Wright, M.D.6    Tarlinton, D.7    Robb, L.8
  • 190
    • 43949157081 scopus 로고
    • The CD19/CD21 signal transduction complex of B lymphocytes
    • Tedder TF, Zhou LJ, Engel P (1994) The CD19/CD21 signal transduction complex of B lymphocytes. Immunol Today 15:437-442
    • (1994) Immunol Today , vol.15 , pp. 437-442
    • Tedder, T.F.1    Zhou, L.J.2    Engel, P.3
  • 191
    • 50249122663 scopus 로고    scopus 로고
    • Catch bonds in adhesion
    • Thomas W (2008) Catch bonds in adhesion. Annu Rev Biomed Eng 10:39-57
    • (2008) Annu Rev Biomed Eng , vol.10 , pp. 39-57
    • Thomas, W.1
  • 192
    • 34247184670 scopus 로고    scopus 로고
    • Ganglioside GM2-tetraspanin CD82 complex inhibits met and its cross-talk with integrins, providing a basis for control of cell motility through glycosynapse
    • Todeschini AR, Dos Santos JN, Handa K, Hakomori SI (2007) Ganglioside GM2-tetraspanin CD82 complex inhibits met and its cross-talk with integrins, providing a basis for control of cell motility through glycosynapse. J Biol Chem 282:8123-8133
    • (2007) J Biol Chem , vol.282 , pp. 8123-8133
    • Todeschini, A.R.1    Dos Santos, J.N.2    Handa, K.3    Hakomori, S.I.4
  • 193
    • 0033431676 scopus 로고    scopus 로고
    • Association of a tetraspanin CD9 with CD5 on the T cell surface: Role of particular transmembrane domains in the association
    • Toyo-Oka K, Yashiro-Ohtani Y, Park CS, Tai XG, Miyake K, Hamaoka T, Fujiwara H (1999) Association of a tetraspanin CD9 with CD5 on the T cell surface: role of particular transmembrane domains in the association. Int Immunol 11:2043-2052
    • (1999) Int Immunol , vol.11 , pp. 2043-2052
    • Toyo-Oka, K.1    Yashiro-Ohtani, Y.2    Park, C.S.3    Tai, X.G.4    Miyake, K.5    Hamaoka, T.6    Fujiwara, H.7
  • 195
    • 0036911337 scopus 로고    scopus 로고
    • Specific heterodimer formation is a prerequisite for uroplakins to exit from the endoplasmic reticulum
    • Tu L, Sun TT, Kreibich G (2002) Specific heterodimer formation is a prerequisite for uroplakins to exit from the endoplasmic reticulum. Mol Biol Cell 13:4221-4230
    • (2002) Mol Biol Cell , vol.13 , pp. 4221-4230
    • Tu, L.1    Sun, T.T.2    Kreibich, G.3
  • 196
    • 78649684704 scopus 로고    scopus 로고
    • Present and future of membrane protein structure determination by electron crystallography
    • Ubarretxena-Belandia I, Stokes DL (2010) Present and future of membrane protein structure determination by electron crystallography. Adv Protein Chem Struct Biol 81:33-60
    • (2010) Adv Protein Chem Struct Biol , vol.81 , pp. 33-60
    • Ubarretxena-Belandia, I.1    Stokes, D.L.2
  • 197
    • 33846052285 scopus 로고    scopus 로고
    • The tetraspanin CD9 mediates lateral association of MHC class II molecules on the dendritic cell surface
    • Unternaehrer JJ, Chow A, Pypaert M, Inaba K, Mellman I (2007) The tetraspanin CD9 mediates lateral association of MHC class II molecules on the dendritic cell surface. Proc Natl Acad Sci USA 104:234-239
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 234-239
    • Unternaehrer, J.J.1    Chow, A.2    Pypaert, M.3    Inaba, K.4    Mellman, I.5
  • 202
    • 35448931927 scopus 로고    scopus 로고
    • Suppression of epidermal growth factor receptor signaling by protein kinase C-alpha activation requires CD82, caveolin-1, and ganglioside
    • Wang XQ, Yan Q, Sun P, Liu JW, Go L, McDaniel SM, Paller AS (2007) Suppression of epidermal growth factor receptor signaling by protein kinase C-alpha activation requires CD82, caveolin-1, and ganglioside. Cancer Res 67:9986-9995
    • (2007) Cancer Res , vol.67 , pp. 9986-9995
    • Wang, X.Q.1    Yan, Q.2    Sun, P.3    Liu, J.W.4    Go, L.5    McDaniel, S.M.6    Paller, A.S.7
  • 203
    • 0037148519 scopus 로고    scopus 로고
    • Murine CD9 is the receptor for pregnancy-specific glycoprotein 17
    • Waterhouse R, Ha C, Dveksler GS (2002) Murine CD9 is the receptor for pregnancy-specific glycoprotein 17. J Exp Med 195:277-282
    • (2002) J Exp Med , vol.195 , pp. 277-282
    • Waterhouse, R.1    Ha, C.2    Dveksler, G.S.3
  • 204
    • 33744763348 scopus 로고    scopus 로고
    • A critical role for tetraspanin CD151 in alpha3beta1 and alpha6beta4 integrin-dependent tumor cell functions on laminin-5
    • Winterwood NE, Varzavand A, Meland MN, Ashman LK, Stipp CS (2006) A critical role for tetraspanin CD151 in alpha3beta1 and alpha6beta4 integrin-dependent tumor cell functions on laminin-5. Mol Biol Cell 17:2707-2721
    • (2006) Mol Biol Cell , vol.17 , pp. 2707-2721
    • Winterwood, N.E.1    Varzavand, A.2    Meland, M.N.3    Ashman, L.K.4    Stipp, C.S.5
  • 206
    • 8144230161 scopus 로고    scopus 로고
    • Tetraspanin microdomains in immune cell signalling and malignant disease
    • Wright MD, Moseley GW, van Spriel AB (2004b) Tetraspanin microdomains in immune cell signalling and malignant disease. Tissue Antigens 64:533-542
    • (2004) Tissue Antigens , vol.64 , pp. 533-542
    • Wright, M.D.1    Moseley, G.W.2    Van Spriel, A.B.3
  • 208
    • 1842614338 scopus 로고    scopus 로고
    • A lysosomal tetraspanin associated with retinal degeneration identified via a genome-wide screen
    • Xu H, Lee SJ, Suzuki E, Dugan KD, Stoddard A, Li HS, Chodosh LA, Montell C (2004) A lysosomal tetraspanin associated with retinal degeneration identified via a genome-wide screen. EMBO J 23:811-822
    • (2004) EMBO J , vol.23 , pp. 811-822
    • Xu, H.1    Lee, S.J.2    Suzuki, E.3    Dugan, K.D.4    Stoddard, A.5    Li, H.S.6    Chodosh, L.A.7    Montell, C.8
  • 209
    • 70350528991 scopus 로고    scopus 로고
    • Tetraspanin12 regulates ADAM 10-dependent cleavage of amyloid precursor protein
    • Xu D, Sharma C, Hemler ME (2009) Tetraspanin12 regulates ADAM 10-dependent cleavage of amyloid precursor protein. FASEB J 23:3674-3681
    • (2009) FASEB J , vol.23 , pp. 3674-3681
    • Xu, D.1    Sharma, C.2    Hemler, M.E.3
  • 211
    • 58149150978 scopus 로고    scopus 로고
    • Probing the interaction of tetraspanin CD151 with integrin alpha 3 beta 1 using a panel of monoclonal antibodies with distinct reactivities toward the CD151-integrin alpha 3 beta 1 complex
    • Yamada M, Tamura Y, Sanzen N, Sato-Nishiuchi R, Hasegawa H, Ashman LK, Rubinstein E, Yanez-Mo M, Sanchez-Madrid F, Sekiguchi K (2008b) Probing the interaction of tetraspanin CD151 with integrin alpha 3 beta 1 using a panel of monoclonal antibodies with distinct reactivities toward the CD151-integrin alpha 3 beta 1 complex. Biochem J 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
  • 213
    • 0036198534 scopus 로고    scopus 로고
    • Palmitoylation of tetraspanin proteins: Modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology
    • Yang X, Claas C, Kraeft SK, Chen LB, Wang Z, Kreidberg JA, Hemler ME (2002) Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology. Mol Biol Cell 13:767-781
    • (2002) Mol Biol Cell , vol.13 , pp. 767-781
    • Yang, X.1    Claas, C.2    Kraeft, S.K.3    Chen, L.B.4    Wang, Z.5    Kreidberg, J.A.6    Hemler, M.E.7
  • 215
    • 0031660652 scopus 로고    scopus 로고
    • Highly stoichiometric, stable, and specific association of integrin alpha3beta1 with CD151 provides a major link to phosphatidylinositol 4-kinase, and may regulate cell migration
    • Yauch RL, Berditchevski F, Harler MB, Reichner J, Hemler ME (1998) Highly stoichiometric, stable, and specific association of integrin alpha3beta1 with CD151 provides a major link to phosphatidylinositol 4-kinase, and may regulate cell migration. Mol Biol Cell 9:2751-2765
    • (1998) Mol Biol Cell , vol.9 , pp. 2751-2765
    • Yauch, R.L.1    Berditchevski, F.2    Harler, M.B.3    Reichner, J.4    Hemler, M.E.5
  • 216
    • 0034737471 scopus 로고    scopus 로고
    • Direct extracellular contact between integrin alpha(3)beta(1) and TM4SF protein CD151
    • Yauch RL, Kazarov AR, Desai B, Lee RT, Hemler ME (2000) Direct extracellular contact between integrin alpha(3)beta(1) and TM4SF protein CD151. J Biol Chem 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
  • 217
    • 40449100704 scopus 로고    scopus 로고
    • A CD63 mutant inhibits T-cell tropic human immunodeficiency virus type 1 entry by disrupting CXCR4 trafficking to the plasma membrane
    • Yoshida T, Kawano Y, Sato K, Ando Y, Aoki J, Miura Y, Komano J, Tanaka Y, Koyanagi Y (2008) A CD63 mutant inhibits T-cell tropic human immunodeficiency virus type 1 entry by disrupting CXCR4 trafficking to the plasma membrane. Traffic 9:540-558
    • (2008) Traffic , vol.9 , pp. 540-558
    • Yoshida, T.1    Kawano, Y.2    Sato, K.3    Ando, Y.4    Aoki, J.5    Miura, Y.6    Komano, J.7    Tanaka, Y.8    Koyanagi, Y.9
  • 218
    • 79953203957 scopus 로고    scopus 로고
    • Structure-function analysis of tetraspanin CD151 reveals distinct requirements for tumor cell behaviors mediated by α31 versus α64 integrin
    • Zevian S, Winterwood NE, Stipp CS (2011) Structure-function analysis of tetraspanin CD151 reveals distinct requirements for tumor cell behaviors mediated by α31 versus α64 integrin. J Biol Chem 286:7496-7506
    • (2011) J Biol Chem , vol.286 , pp. 7496-7506
    • Zevian, S.1    Winterwood, N.E.2    Stipp, C.S.3
  • 219
    • 0035816663 scopus 로고    scopus 로고
    • Transmembrane-4 superfamily proteins associate with activated Protein Kinase C (PKC) and link PKC to specific beta(1) integrins
    • Zhang XA, Bontrager AL, Hemler ME (2001) Transmembrane-4 superfamily proteins associate with activated Protein Kinase C (PKC) and link PKC to specific beta(1) integrins. J Biol Chem 276:25005-25013
    • (2001) J Biol Chem , vol.276 , pp. 25005-25013
    • Zhang, X.A.1    Bontrager, A.L.2    Hemler, M.E.3
  • 221
    • 0038179866 scopus 로고    scopus 로고
    • EWI2/PGRL associates with the metastasis suppressor KAI1/CD82 and inhibits the migration of prostate cancer cells
    • Zhang XA, Lane WS, Charrin S, Rubinstein E, Liu L (2003) EWI2/PGRL associates with the metastasis suppressor KAI1/CD82 and inhibits the migration of prostate cancer cells. Cancer Res 63:2665-2674
    • (2003) Cancer Res , vol.63 , pp. 2665-2674
    • Zhang, X.A.1    Lane, W.S.2    Charrin, S.3    Rubinstein, E.4    Liu, L.5
  • 222
    • 5644243063 scopus 로고    scopus 로고
    • The palmitoylation of metastasis suppressor KAI1/CD82 is important for its motility-and invasiveness-inhibitory activity
    • Zhou B, Liu L, Reddivari M, Zhang XA (2004) The palmitoylation of metastasis suppressor KAI1/CD82 is important for its motility-and invasiveness-inhibitory activity. Cancer Res 64:7455-7463
    • (2004) Cancer Res , vol.64 , pp. 7455-7463
    • Zhou, B.1    Liu, L.2    Reddivari, M.3    Zhang, X.A.4
  • 224
    • 57749169272 scopus 로고    scopus 로고
    • Tetraspanins: Push and pull in suppressing and promoting metastasis
    • Zoller M (2009) Tetraspanins: push and pull in suppressing and promoting metastasis. Nat Rev Cancer 9:40-55
    • (2009) Nat Rev Cancer , vol.9 , pp. 40-55
    • Zoller, M.1
  • 225
    • 77954464439 scopus 로고    scopus 로고
    • Activation of the ERK signaling pathway is involved in CD151-induced angiogenic effects on the formation of CD151-integrin complexes
    • Zuo HJ, Lin JY, Liu ZY, Liu WF, Liu T, Yang J, Liu Y, Wang DW, Liu ZX (2010) Activation of the ERK signaling pathway is involved in CD151-induced angiogenic effects on the formation of CD151-integrin complexes. Acta Pharmacol Sin 31:805-812
    • (2010) Acta Pharmacol Sin , vol.31 , pp. 805-812
    • Zuo, H.J.1    Lin, J.Y.2    Liu, Z.Y.3    Liu, W.F.4    Liu, T.5    Yang, J.6    Liu, Y.7    Wang, D.W.8    Liu, Z.X.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.