메뉴 건너뛰기




Volumn 39, Issue 2, 2011, Pages 547-552

Tetraspanin protein contributions to cancer

Author keywords

4 integrin; A disintegrin and metalloproteinase 10 (ADAM10); CD151; CD9; EWI 2; EWI F; Tetraspanin; Tspan12

Indexed keywords

ADAM10 ENDOPEPTIDASE; ALPHA6BETA4 INTEGRIN; CD151 ANTIGEN; CD9 ANTIGEN; DISINTEGRIN; EWI 2 PROTEIN; EWI F PROTEIN; MEMBRANE PROTEIN; TETRASPANIN; TSPAN12 PROTEIN; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 6;

EID: 79953195584     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0390547     Document Type: Review
Times cited : (76)

References (79)
  • 1
    • 0030975429 scopus 로고    scopus 로고
    • Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: Comparison with CD9, CD63, and α5β1 integrin
    • Sincock, P.M., Mayrohofer, G. and Ashman, L.K. (1997) Localization of the transmembrane 4 superfamily (TM4SF) member PETA-3 (CD151) in normal human tissues: comparison with CD9, CD63, and α5β1 integrin. J. Histochem. Cytochem. 45, 515-525 (Pubitemid 27175796)
    • (1997) Journal of Histochemistry and Cytochemistry , vol.45 , Issue.4 , pp. 515-525
    • Sincock, P.M.1    Mayrhofer, G.2    Ashman, L.K.3
  • 3
    • 33846895645 scopus 로고    scopus 로고
    • Deletion of tetraspanin Cd151 results in decreased pathologic angiogenesis in vivo and in vitro
    • DOI 10.1182/blood-2006-08-041970
    • Takeda, Y., Kazarov, A.R., Butterfield, C.E., Hopkins, B.D., Benjamin, L.E., Kaipainen, A. and Hemler, M.E. (2007) Deletion of tetraspanin Cd151 results in decreased pathologic angiogenesis in vivo and in vitro. Blood 109, 1524-1532 (Pubitemid 46239585)
    • (2007) Blood , vol.109 , Issue.4 , pp. 1524-1532
    • Takeda, Y.1    Kazarov, A.R.2    Butterfield, C.E.3    Hopkins, B.D.4    Benjamin, L.E.5    Kaipainen, A.6    Hemler, M.E.7
  • 5
    • 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, R.M., Guthrie, P.L., Gubler, M.C., Ashman, L.K. and 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
  • 7
    • 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
    • DOI 10.1182/blood-2004-04-1512
    • Karamatic, CV, Burton, N., Kagan, A., Green, C.A., Levene, C., Flinter, F., Brady, L.R., Daniels, G. and Anstee, D.J. (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 (Pubitemid 39331816)
    • (2004) Blood , vol.104 , Issue.8 , pp. 2217-2223
    • Crew, V.K.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
  • 8
    • 0023936616 scopus 로고
    • Occurrence of hereditary nephritis, pretibial epidermolysis bullosa and β-thalassemia minor in two siblings with end-stage renal disease
    • Kagan, A., Feld, S., Chemke, J. and Bar-Khayim, Y. (1988) Occurrence of hereditary nephritis, pretibial epidermolysis bullosa and β-thalassemia minor in two siblings with end-stage renal disease. Nephron 49, 331-332
    • (1988) Nephron , vol.49 , pp. 331-332
    • Kagan, A.1    Feld, S.2    Chemke, J.3    Bar-Khayim, Y.4
  • 9
    • 0037087710 scopus 로고    scopus 로고
    • Association of the tetraspanin CD151 with the laminin-binding integrins α3β1, α6β1, α6β4 and β7α1 in cells in culture and in vivo
    • Sterk, L.M., Geuijen, C.A., Van Den Berg, J.G., Claessen, N., Weening, J.J. and Sonnenberg, A. (2002) Association of the tetraspanin CD151 with the laminin-binding integrins α3β1, α6β1, α6β4 and β7α1 in cells in culture and in vivo. J. Cell Sci. 115, 1161-1173 (Pubitemid 34272481)
    • (2002) Journal of Cell Science , vol.115 , Issue.6 , pp. 1161-1173
    • Sterk, L.M.T.1    Geuijen, C.A.W.2    Van Den, B.J.G.3    Claessen, N.4    Weening, J.J.5    Sonnenberg, A.6
  • 10
    • 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., Berditchevski, F., Harler, M.B., Reichner, J. and Hemler, M.E. (1998) 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, 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
  • 11
    • 0035816663 scopus 로고    scopus 로고
    • TM4SF proteins associate with activated PKC and link PKC to specific β1 integrins
    • Zhang, X.A., Bontrager, A.L. and Hemler, M.E. (2001) TM4SF proteins associate with activated PKC and link PKC to specific β1 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
  • 12
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler, M.E. (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
  • 13
    • 35748975965 scopus 로고    scopus 로고
    • Tetraspanin CD151 promotes cell migration by regulating integrin trafficking
    • Liu, L., He, B., Liu, W.M., Zhou, D., Cox, J.V. and Zhang, X.A. (2007) Tetraspanin CD151 promotes cell migration by regulating integrin trafficking. J. Biol. Chem. 282, 31631-31642
    • (2007) J. Biol. Chem. , vol.282 , pp. 31631-31642
    • Liu, L.1    He, B.2    Liu, W.M.3    Zhou, D.4    Cox, J.V.5    Zhang, X.A.6
  • 14
    • 72949119124 scopus 로고    scopus 로고
    • Integrins in cancer: Biological implications and therapeutic opportunities
    • Desgrosellier, J.S. and Cheresh, D.A. (2010) Integrins in cancer: biological implications and therapeutic opportunities. Nat. Rev. Cancer 10, 9-22
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 9-22
    • Desgrosellier, J.S.1    Cheresh, D.A.2
  • 15
    • 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
  • 18
    • 77955022593 scopus 로고    scopus 로고
    • Tetraspanin CD151 regulates transforming growth factor β signaling: Implication in tumor metastasis
    • Sadej, R., Romanska, H., Kavanagh, D., Baldwin, G., Takahashi, T., Kalia, N. and Berditchevski, F. (2010) Tetraspanin CD151 regulates transforming growth factor β signaling: implication in tumor metastasis. Cancer Res. 70, 6059-6070
    • (2010) Cancer Res. , vol.70 , pp. 6059-6070
    • Sadej, R.1    Romanska, H.2    Kavanagh, D.3    Baldwin, G.4    Takahashi, T.5    Kalia, N.6    Berditchevski, F.7
  • 19
    • 61949226823 scopus 로고    scopus 로고
    • Role of overexpression of CD151 and/or c-Met in predicting prognosis of hepatocellular carcinoma
    • Ke, A.W., Shi, G.M., Zhou, J., Wu, F.Z., Ding, Z.B., Hu, M.Y., Xu, Y., Song, Z.J., Wang, Z.J., Wu, J.C. et al. (2009) Role of overexpression of CD151 and/or c-Met in predicting prognosis of hepatocellular carcinoma. Hepatology 49, 491-503
    • (2009) Hepatology , vol.49 , pp. 491-503
    • Ke, A.W.1    Shi, G.M.2    Zhou, J.3    Wu, F.Z.4    Ding, Z.B.5    Hu, M.Y.6    Xu, Y.7    Song, Z.J.8    Wang, Z.J.9    Wu, J.C.10
  • 20
    • 77954229566 scopus 로고    scopus 로고
    • CD151 modulates expression of matrix metalloproteinase 9 and promotes neoangiogenesis and progression of hepatocellular carcinoma
    • Shi, G.M., Ke, A.W., Zhou, J., Wang, X.Y., Xu, Y., Ding, Z.B., Devbhandari, R.P., Huang, X.Y., Qiu, S.J., Shi, Y.H. et al. (2010) CD151 modulates expression of matrix metalloproteinase 9 and promotes neoangiogenesis and progression of hepatocellular carcinoma. Hepatology 52, 183-196
    • (2010) Hepatology , vol.52 , pp. 183-196
    • Shi, G.M.1    Ke, A.W.2    Zhou, J.3    Wang, X.Y.4    Xu, Y.5    Ding, Z.B.6    Devbhandari, R.P.7    Huang, X.Y.8    Qiu, S.J.9    Shi, Y.H.10
  • 21
    • 39849083927 scopus 로고    scopus 로고
    • The Inhibition of Tumor Cell Intravasation and Subsequent Metastasis via Regulation of in Vivo Tumor Cell Motility by the Tetraspanin CD151
    • DOI 10.1016/j.ccr.2008.01.031, PII S1535610808000408
    • Zijlstra, A., Lewis, J., Degryse, B., Stuhlmann, H. and Quigley, J.P. (2008) The inhibition of tumor cell intravasation and subsequent metastasis via regulation of in vivo tumor cell motility by the tetraspanin CD151. Cancer Cell 13, 221-234 (Pubitemid 351318371)
    • (2008) Cancer Cell , vol.13 , Issue.3 , pp. 221-234
    • Zijlstra, A.1    Lewis, J.2    DeGryse, B.3    Stuhlmann, H.4    Quigley, J.P.5
  • 23
    • 77950257304 scopus 로고    scopus 로고
    • Disruption of laminin-integrin-CD151-focal adhesion kinase axis sensitizes breast cancer cells to ErbB2 antagonists
    • Yang, X.H., Flores, L.M., Li, Q., Zhou, P., Xu, F., Krop, I.E. and Hemler, M.E. (2010) Disruption of laminin-integrin-CD151-focal adhesion kinase axis sensitizes breast cancer cells to ErbB2 antagonists. Cancer Res. 70, 2256-2263
    • (2010) Cancer Res. , vol.70 , pp. 2256-2263
    • Yang, X.H.1    Flores, L.M.2    Li, Q.3    Zhou, P.4    Xu, F.5    Krop, I.E.6    Hemler, M.E.7
  • 24
    • 2942628076 scopus 로고    scopus 로고
    • Protein kinase Cα phosphorylation of specific serines in the connecting segment of the β4 integrin regulates the dynamics of type II hemidesmosomes
    • Rabinovitz, I., Tsomo, L. and Mercurio, A.M. (2004) Protein kinase Cα phosphorylation of specific serines in the connecting segment of the β4 integrin regulates the dynamics of type II hemidesmosomes. Mol. Cell. Biol. 24, 4351-4360
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4351-4360
    • Rabinovitz, I.1    Tsomo, L.2    Mercurio, A.M.3
  • 25
    • 34548477663 scopus 로고    scopus 로고
    • Serine phosphorylation of the integrin β4 subunit is necessary for epidermal growth factor receptor induced hemidesmosome disruption
    • Wilhelmsen, K., Litjens, S.H., Kuikman, I., Margadant, C., van Rheenen, J. and Sonnenberg, A. (2007) Serine phosphorylation of the integrin β4 subunit is necessary for epidermal growth factor receptor induced hemidesmosome disruption. Mol. Biol. Cell 18, 3512-3522
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3512-3522
    • Wilhelmsen, K.1    Litjens, S.H.2    Kuikman, I.3    Margadant, C.4    Van Rheenen, J.5    Sonnenberg, A.6
  • 26
    • 63049113014 scopus 로고    scopus 로고
    • Phosphorylation of a novel site on the β4 integrin at the trailing edge of migrating cells promotes hemidesmosome disassembly
    • Germain, E.C., Santos, T.M. and Rabinovitz, I. (2009) Phosphorylation of a novel site on the β4 integrin at the trailing edge of migrating cells promotes hemidesmosome disassembly. Mol. Biol. Cell 20, 56-67
    • (2009) Mol. Biol. Cell , vol.20 , pp. 56-67
    • Germain, E.C.1    Santos, T.M.2    Rabinovitz, I.3
  • 27
    • 34748863597 scopus 로고    scopus 로고
    • Targeting integrin β4 for cancer and anti-angiogenic therapy
    • Giancotti, F.G. (2007) Targeting integrin β4 for cancer and anti-angiogenic therapy. Trends Pharmacol. Sci. 28, 506-511
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 506-511
    • Giancotti, F.G.1
  • 28
    • 0035847016 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the β4 integrin cytoplasmic domain mediates Shc signaling to extracellular signal-regulated kinase and antagonizes formation of hemidesmosomes
    • Dans, M., Gagnoux-Palacios, L., Blaikie, P., Klein, S., Mariotti, A. and Giancotti, F.G. (2001) Tyrosine phosphorylation of the β4 integrin cytoplasmic domain mediates Shc signaling to extracellular signal-regulated kinase and antagonizes formation of hemidesmosomes. J. Biol. Chem. 276, 1494-1502
    • (2001) J. Biol. Chem. , vol.276 , pp. 1494-1502
    • Dans, M.1    Gagnoux-Palacios, L.2    Blaikie, P.3    Klein, S.4    Mariotti, A.5    Giancotti, F.G.6
  • 29
    • 0034951677 scopus 로고    scopus 로고
    • Identification of insulin receptor substrate 1 (IRS-1) and IRS-2 as signaling intermediates in the α6β4 integrin-dependent activation of phosphoinositide 3-OH kinase and promotion of invasion
    • Shaw, L.M. (2001) Identification of insulin receptor substrate 1 (IRS-1) and IRS-2 as signaling intermediates in the α6β4 integrin-dependent activation of phosphoinositide 3-OH kinase and promotion of invasion. Mol. Cell. Biol. 21, 5082-5093
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5082-5093
    • Shaw, L.M.1
  • 30
    • 11244304502 scopus 로고    scopus 로고
    • Palmitoylation supports assembly and function of integrin-tetraspanin complexes
    • DOI 10.1083/jcb.200404100
    • Yang, X., Kovalenko, O.V., Tang, W., Claas, C., Stipp, C.S. and Hemler, M.E. (2004) Palmitoylation supports assembly and function of integrin-tetraspanin complexes. J. Cell Biol. 167, 1231-1240 (Pubitemid 40066636)
    • (2004) Journal of Cell Biology , vol.167 , Issue.6 , pp. 1231-1240
    • Yang, X.1    Kovalenko, O.V.2    Tang, W.3    Claas, C.4    Stipp, C.S.5    Hemler, M.E.6
  • 32
    • 33745947286 scopus 로고    scopus 로고
    • Current insights into the formation and breakdown of hemidesmosomes
    • DOI 10.1016/j.tcb.2006.05.004, PII S0962892406001395
    • Litjens, S.H., de Pereda, J.M. and Sonnenberg, A. (2006) Current insights into the formation and breakdown of hemidesmosomes. Trends Cell Biol. 16, 376-383 (Pubitemid 44062316)
    • (2006) Trends in Cell Biology , vol.16 , Issue.7 , pp. 376-383
    • Litjens, S.H.M.1    De Pereda, J.M.2    Sonnenberg, A.3
  • 33
    • 0034333146 scopus 로고    scopus 로고
    • Integrins as receptors for laminins
    • Belkin, A.M. and Stepp, M.A. (2000) Integrins as receptors for laminins. Microsc. Res. Tech. 51, 280-301
    • (2000) Microsc. Res. Tech. , vol.51 , pp. 280-301
    • Belkin, A.M.1    Stepp, M.A.2
  • 34
    • 0032841440 scopus 로고    scopus 로고
    • The aα3 laminin subunit, α6β4 and α3β1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin
    • Goldfinger, L.E., Hopkinson, S.B., deHart, G.W., Collawn, S., Couchman, J.R. and Jones, J.C. (1999) The aα3 laminin subunit, α6β4 and α3β1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin. J. Cell Sci. 112, 2615-2629
    • (1999) J. Cell Sci. , vol.112 , pp. 2615-2629
    • Goldfinger, L.E.1    Hopkinson, S.B.2    DeHart, G.W.3    Collawn, S.4    Couchman, J.R.5    Jones, J.C.6
  • 35
    • 0031024817 scopus 로고    scopus 로고
    • The role of laminin-5 and its receptors in mammary epithelial cell branching morphogenesis
    • Stahl, S., Weitzman, S. and Jones, J.C. (1997) The role of laminin-5 and its receptors in mammary epithelial cell branching morphogenesis. J. Cell Sci. 110, 55-63 (Pubitemid 27057944)
    • (1997) Journal of Cell Science , vol.110 , Issue.1 , pp. 55-63
    • Stahl, S.1    Weitzman, S.2    Jones, J.C.R.3
  • 36
    • 0036726312 scopus 로고    scopus 로고
    • β4 integrin-dependent formation of polarized three-dimensional architecture confers resistance to apoptosis in normal and malignant mammary epithelium
    • DOI 10.1016/S1535-6108(02)00125-3
    • Weaver, V.M., Lelievre, S., Lakins, J.N., Chrenek, M.A., Jones, J.C., Giancotti, F., Werb, Z. and Bissell, M.J. (2002) β4 Integrin-dependent formation of polarized three-dimensional architecture confers resistance to apoptosis in normal and malignant mammary epithelium. Cancer Cell 2, 205-216 (Pubitemid 41043976)
    • (2002) Cancer Cell , vol.2 , Issue.3 , pp. 205-216
    • Weaver, V.M.1    Lelievre, S.2    Lakins, J.N.3    Chrenek, M.A.4    Jones, J.C.R.5    Giancotti, F.6    Werb, Z.7    Bissell, M.J.8
  • 37
    • 0028813315 scopus 로고
    • High expression level of α6 integrin in human breast carcinoma is correlated with reduced survival
    • Friedrichs, K., Ruiz, P., Franke, F., Gille, I., Terpe, H.-J. and Imhof, B.A. (1995) High expression level of α6 integrin in human breast carcinoma is correlated with reduced survival. Cancer Res. 55, 901-906
    • (1995) Cancer Res. , vol.55 , pp. 901-906
    • Friedrichs, K.1    Ruiz, P.2    Franke, F.3    Gille, I.4    Terpe, H.-J.5    Imhof, B.A.6
  • 38
    • 0031914189 scopus 로고    scopus 로고
    • Prognostic value of α6β4 integrin expression in breast carcinomas is affected by laminin production from tumor cells
    • Tagliabue, E., Ghirelli, C., Squicciarini, P., Aiello, P., Colnaghi, M.I. and Menard, S. (1998) Prognostic value of α6β4 integrin expression in breast carcinomas is affected by laminin production from tumor cells. Clin. Cancer Res. 4, 407-410
    • (1998) Clin. Cancer Res. , vol.4 , pp. 407-410
    • Tagliabue, E.1    Ghirelli, C.2    Squicciarini, P.3    Aiello, P.4    Colnaghi, M.I.5    Menard, S.6
  • 39
    • 0033147378 scopus 로고    scopus 로고
    • Increased levels of α6 integrins are associated with the metastatic phenotype of human breast cancer cells
    • Mukhopadhyay, R., Theriault, R.L. and Price, J.E. (1999) Increased levels of α6 integrins are associated with the metastatic phenotype of human breast cancer cells. Clin. Exp. Metastasis 17, 325-332
    • (1999) Clin. Exp. Metastasis , vol.17 , pp. 325-332
    • Mukhopadhyay, R.1    Theriault, R.L.2    Price, J.E.3
  • 40
    • 0030695152 scopus 로고    scopus 로고
    • The integrin α6β1 promotes the survival of metastatic human breast carcinoma cells in mice
    • Wewer, U.M., Shaw, L.M., Albrechtsen, R. and Mercurio, A.M. (1997) The integrin α6β1 promotes the survival of metastatic human breast carcinoma cells in mice. Am. J. Pathol. 151, 1191-1198
    • (1997) Am. J. Pathol. , vol.151 , pp. 1191-1198
    • Wewer, U.M.1    Shaw, L.M.2    Albrechtsen, R.3    Mercurio, A.M.4
  • 41
    • 3242781896 scopus 로고    scopus 로고
    • Integrin clipping: A novel adhesion switch?
    • Demetriou, M.C. and Cress, A.E. (2004) Integrin clipping: a novel adhesion switch? J. Cell. Biochem. 91, 26-35
    • (2004) J. Cell. Biochem. , vol.91 , pp. 26-35
    • Demetriou, M.C.1    Cress, A.E.2
  • 42
    • 3442897659 scopus 로고    scopus 로고
    • Contributions of the α6 integrins to breast carcinoma survival and progression
    • Chung, J. and Mercurio, A.M. (2004) Contributions of the α6 integrins to breast carcinoma survival and progression. Mol. Cells 17, 203-209 (Pubitemid 39137066)
    • (2004) Molecules and Cells , vol.17 , Issue.2 , pp. 203-209
    • Chung, J.1    Mercurio, A.M.2
  • 43
    • 0035019920 scopus 로고    scopus 로고
    • Towards a mechanistic understanding of tumor invasion: Lessons from the α6β4 integrin
    • Mercurio, A.M. and Rabinovitz, I. (2001) Towards a mechanistic understanding of tumor invasion: lessons from the α6β4 integrin. Semin. Cancer Biol. 11, 129-141
    • (2001) Semin. Cancer Biol. , vol.11 , pp. 129-141
    • Mercurio, A.M.1    Rabinovitz, I.2
  • 45
    • 0033615961 scopus 로고    scopus 로고
    • p53 inhibits α6β4 integrin survival signaling by promoting the caspase 3-dependent cleavage of Akt/PKB
    • Bachelder, R.E., Ribick, M.J., Marchetti, A., Falcioni, R., Soddu, S., Davis, K.R. and Mercurio, A.M. (1999) p53 inhibits α6β4 integrin survival signaling by promoting the caspase 3-dependent cleavage of Akt/PKB. J. Cell Biol. 147, 1063-1072
    • (1999) J. Cell Biol. , vol.147 , pp. 1063-1072
    • Bachelder, R.E.1    Ribick, M.J.2    Marchetti, A.3    Falcioni, R.4    Soddu, S.5    Davis, K.R.6    Mercurio, A.M.7
  • 47
    • 33746764457 scopus 로고    scopus 로고
    • β4 Integrin Amplifies ErbB2 Signaling to Promote Mammary Tumorigenesis
    • DOI 10.1016/j.cell.2006.05.047, PII S009286740600907X
    • Guo, W., Pylayeva, Y., Pepe, A., Yoshioka, T., Muller, W.J., Inghirami, G. and Giancotti, F.G. (2006) β4 Integrin amplifies ErbB2 signaling to promote mammary tumorigenesis. Cell 126, 489-502 (Pubitemid 44163602)
    • (2006) Cell , vol.126 , Issue.3 , pp. 489-502
    • Guo, W.1    Pylayeva, Y.2    Pepe, A.3    Yoshioka, T.4    Muller, W.J.5    Inghirami, G.6    Giancotti, F.G.7
  • 48
    • 7944224012 scopus 로고    scopus 로고
    • Integrin β4 signaling promotes tumor angiogenesis
    • DOI 10.1016/j.ccr.2004.09.029, PII S1535610804002995
    • Nikolopoulos, S.N., Blaikie, P., Yoshioka, T., Guo, W. and Giancotti, F.G. (2004) Integrin β4 signaling promotes tumor angiogenesis. Cancer Cell 6, 471-483 (Pubitemid 39469983)
    • (2004) Cancer Cell , vol.6 , Issue.5 , pp. 471-483
    • Nikolopoulos, S.N.1    Blaikie, P.2    Yoshioka, T.3    Guo, W.4    Giancotti, F.G.5
  • 49
    • 33748958810 scopus 로고    scopus 로고
    • Systematic screening for palmitoyl transferase activity of the DHHC protein family in mammalian cells
    • DOI 10.1016/j.ymeth.2006.05.015, PII S1046202306001538, Protein Palmitoylation
    • Fukata, Y., Iwanaga, T. and Fukata, M. (2006) Systematic screening for palmitoyl transferase activity of the DHHC protein family in mammalian cells. Methods 40, 177-182 (Pubitemid 44442975)
    • (2006) Methods , vol.40 , Issue.2 , pp. 177-182
    • Fukata, Y.1    Iwanaga, T.2    Fukata, M.3
  • 50
    • 33744826797 scopus 로고    scopus 로고
    • Protein palmitoylation by a family of DHHC protein S-acyltransferases
    • DOI 10.1194/jlr.R600007-JLR200
    • Mitchell, D.A., Vasudevan, A., Linder, M.E. and Deschenes, R.J. (2006) Protein palmitoylation by a family of DHHC protein S-acyltransferases. J. Lipid Res. 47, 1118-1127 (Pubitemid 43830703)
    • (2006) Journal of Lipid Research , vol.47 , Issue.6 , pp. 1118-1127
    • Mitchell, D.A.1    Vasudevan, A.2    Linder, M.E.3    Deschenes, R.J.4
  • 51
    • 0344708475 scopus 로고    scopus 로고
    • Tetraspanin proteins mediate cellular penetration, invasion and fusion events, and define a novel type of membrane microdomain
    • Hemler, M.E. (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
  • 56
    • 0035207920 scopus 로고    scopus 로고
    • Complexes of tetraspanins with integrins: More than meets the eye
    • Berditchevski, F. (2001) Complexes of tetraspanins with integrins: more than meets the eye. J. Cell Sci. 114, 4143-4151
    • (2001) J. Cell Sci. , vol.114 , pp. 4143-4151
    • Berditchevski, F.1
  • 57
    • 0036333987 scopus 로고    scopus 로고
    • Residues SFQ (173-175) in the large extracellular loop of CD9 are required for gamete fusion
    • Zhu, G.Z., Miller, B.J., Boucheix, C., Rubinstein, E., Liu, C.C., Hynes, R.O., Myles, D.G. and Primakoff, P. (2002) Residues SFQ (173-175) in the large extracellular loop of CD9 are required for gamete fusion. Development 129, 1995-2002 (Pubitemid 34874214)
    • (2002) Development , vol.129 , Issue.8 , pp. 1995-2002
    • Zhu, G.-Z.1    Miller, B.J.2    Boucheix, C.3    Rubinstein, E.4    Liu, C.C.5    Hynes, R.O.6    Myles, D.G.7    Primakoff, P.8
  • 58
    • 52649170765 scopus 로고    scopus 로고
    • Tetraspanin family member CD9 inhibits Aggrus/podoplanin-induced platelet aggregation and suppresses pulmonary metastasis
    • Nakazawa, Y., Sato, S., Naito, M., Kato, Y., Mishima, K., Arai, H., Tsuruo, T. and Fujita, N. (2008) Tetraspanin family member CD9 inhibits Aggrus/podoplanin-induced platelet aggregation and suppresses pulmonary metastasis. Blood 112, 1730-1739
    • (2008) Blood , vol.112 , pp. 1730-1739
    • Nakazawa, Y.1    Sato, S.2    Naito, M.3    Kato, Y.4    Mishima, K.5    Arai, H.6    Tsuruo, T.7    Fujita, N.8
  • 59
    • 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. and 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
  • 60
    • 16844366288 scopus 로고    scopus 로고
    • Down-regulation of CD9 in human ovarian carcinoma cell might contribute to peritoneal dissemination: Morphologic alteration and reduced expression of β1 integrin subsets
    • DOI 10.1158/0008-5472.CAN-04-3123
    • Furuya, M., Kato, H., Nishimura, N., Ishiwata, I., Ikeda, H., Ito, R., Yoshiki, T. and Ishikura, H. (2005) Down-regulation of CD9 in human ovarian carcinoma cell might contribute to peritoneal dissemination: morphologic alteration and reduced expression of β1 integrin subsets. Cancer Res. 65, 2617-2625 (Pubitemid 40490060)
    • (2005) Cancer Research , vol.65 , Issue.7 , pp. 2617-2625
    • Furuya, M.1    Kato, H.2    Nishimura, N.3    Ishiwata, I.4    Ikeda, H.5    Ito, R.6    Yoshiki, T.7    Ishikura, H.8
  • 61
    • 0025837201 scopus 로고
    • Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility
    • Miyake, M., Koyama, M., Seno, M. and Ikeyama, S. (1991) Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility. J. Exp. Med. 174, 1347-1354
    • (1991) J. Exp. Med. , vol.174 , pp. 1347-1354
    • Miyake, M.1    Koyama, M.2    Seno, M.3    Ikeyama, S.4
  • 62
    • 0035895069 scopus 로고    scopus 로고
    • Regulatory role of tetraspanin CD9 in tumor-endothelial cell interaction during transendothelial invasion of melanoma cells
    • Longo, N., Yáñez-Mó, M., Mittelbrunn, M., de la Rosa, G., Muñoz, M.L., Sánchez-Madrid, F. and Sánchez-Mateos, P. (2001) Regulatory role of tetraspanin CD9 in tumor-endothelial cell interaction during transendothelial invasion of melanoma cells. Blood 98, 3717-3726
    • (2001) Blood , vol.98 , pp. 3717-3726
    • Longo, N.1    Yáñez-Mó, M.2    Mittelbrunn, M.3    De La Rosa, G.4    Muñoz, M.L.5    Sánchez-Madrid, F.6    Sánchez-Mateos, P.7
  • 64
    • 1542742106 scopus 로고    scopus 로고
    • Tetraspanin CD81 is linked to ERK/MAPKinase signaling by Shc in liver tumor cells
    • DOI 10.1038/sj.onc.1207287
    • Carloni, V., Mazzocca, A. and Ravichandran, K.S. (2004) Tetraspanin CD81 is linked to ERK/MAPKinase signaling by Shc in liver tumor cells. Oncogene 23, 1566-1574 (Pubitemid 38406519)
    • (2004) Oncogene , vol.23 , Issue.8 , pp. 1566-1574
    • Carloni, V.1    Mazzocca, A.2    Ravichandran, K.S.3
  • 65
    • 0034331438 scopus 로고    scopus 로고
    • Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphatidylinositol 4-kinase
    • Yauch, R.L. and Hemler, M.E. (2000) Specific interactions among transmembrane 4 superfamily (TM4SF) proteins and phosphatidylinositol 4-kinase. Biochem. J. 351, 629-637
    • (2000) Biochem. J. , vol.351 , pp. 629-637
    • Yauch, R.L.1    Hemler, M.E.2
  • 66
  • 67
    • 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., Fan, H., Shum, L. and Derynck, R. (2000) The tetraspanin CD9 associates with transmembrane TGF-α and regulates TGF-α-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
  • 68
    • 0035895876 scopus 로고    scopus 로고
    • FPRP: A major, highly stoichiometric, highly specific CD81 and CD9-associated protein
    • Stipp, C.S., Orlicky, D. and Hemler, M.E. (2001) 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
  • 70
    • 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., Kolesnikova, T.V. and Hemler, M.E. (2001) 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
  • 71
    • 1842474884 scopus 로고    scopus 로고
    • EWI-2 modulates lymphocyte integrin α4β1 functions
    • DOI 10.1182/blood-2003-07-2201
    • Kolesnikova, T.V., Stipp, C.S., Rao, R.M., Lane, W.S., Luscinskas, F.W. and Hemler, M.E. (2004) EWI-2 modulates lymphocyte integrin α4β1 functions. Blood 103, 3013-3019 (Pubitemid 38451674)
    • (2004) Blood , vol.103 , Issue.8 , pp. 3013-3019
    • Kolesnikova, T.V.1    Stipp, C.S.2    Rao, R.M.3    Lane, W.S.4    Luscinskas, F.W.5    Hemler, M.E.6
  • 73
    • 70349838225 scopus 로고    scopus 로고
    • TSPAN12 regulates retinal vascular development by promoting Norrin- But not Wnt-induced FZD4/β-catenin signaling
    • Junge, H.J., Yang, S., Burton, J.B., Paes, K., Shu, X., French, D.M., Costa, M., Rice, D.S. and Ye, W. (2009) TSPAN12 regulates retinal vascular development by promoting Norrin- but not Wnt-induced FZD4/β-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
  • 75
    • 77956267435 scopus 로고    scopus 로고
    • The Norrin/Frizzled4 signaling pathway in retinal vascular development and disease
    • Ye, X., Wang, Y. and Nathans, J. (2010) The Norrin/Frizzled4 signaling pathway in retinal vascular development and disease. Trends Mol. Med. 16, 417-425
    • (2010) Trends Mol. Med. , vol.16 , pp. 417-425
    • Ye, X.1    Wang, Y.2    Nathans, J.3
  • 77
    • 70350528991 scopus 로고    scopus 로고
    • Tetraspanin12 regulates ADAM10-dependent cleavage of amyloid precursor protein
    • Xu, D., Sharma, C. and Hemler, M.E. (2009) Tetraspanin12 regulates ADAM10-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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.