메뉴 건너뛰기




Volumn 45, Issue 6, 2013, Pages 1133-1144

The tetraspanin network modulates MT1-MMP cell surface trafficking

Author keywords

Cancer; Cell surface trafficking; MT1 MMP; Protein protein interaction; Tetraspanin

Indexed keywords

CD37 ANTIGEN; CD53 ANTIGEN; CD63 ANTIGEN; CD9 ANTIGEN; MATRIX METALLOPROTEINASE 14; TETRASPANIN;

EID: 84875957382     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2013.02.020     Document Type: Article
Times cited : (32)

References (78)
  • 3
  • 6
    • 33846226473 scopus 로고    scopus 로고
    • Tetraspanins as regulators of protein trafficking
    • F. Berditchevski, and E. Odintsova Tetraspanins as regulators of protein trafficking Traffic 8 2007 89 96
    • (2007) Traffic , vol.8 , pp. 89-96
    • Berditchevski, F.1    Odintsova, E.2
  • 7
    • 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
    • F. Berditchevski, E. Odintsova, S. Sawada, and E. Gilbert 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 Journal of Biological Chemistry 277 2002 36991 37000
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 36991-37000
    • Berditchevski, F.1    Odintsova, E.2    Sawada, S.3    Gilbert, E.4
  • 8
    • 0032567429 scopus 로고    scopus 로고
    • The propeptide domain of membrane type 1 matrix metalloproteinase is required for binding of tissue inhibitor of metalloproteinases and for activation of pro-gelatinase A
    • J. Cao, M. Drews, H.M. Lee, C. Conner, W.F. Bahou, and S. Zucker The propeptide domain of membrane type 1 matrix metalloproteinase is required for binding of tissue inhibitor of metalloproteinases and for activation of pro-gelatinase A Journal of Biological Chemistry 273 1998 34745 34752
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 34745-34752
    • Cao, J.1    Drews, M.2    Lee, H.M.3    Conner, C.4    Bahou, W.F.5    Zucker, S.6
  • 11
    • 0037051906 scopus 로고    scopus 로고
    • Differential stability of tetraspanin/tetraspanin interactions: Role of palmitoylation
    • S. Charrin, S. Manie, M. Oualid, M. Billard, C. Boucheix, and E. Rubinstein Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation FEBS Letters 516 2002 139 144
    • (2002) FEBS Letters , vol.516 , pp. 139-144
    • Charrin, S.1    Manie, S.2    Oualid, M.3    Billard, M.4    Boucheix, C.5    Rubinstein, E.6
  • 13
    • 0035896648 scopus 로고    scopus 로고
    • Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts
    • C. Claas, C.S. Stipp, and M.E. Hemler Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts Journal of Biological Chemistry 276 2001 7974 7984
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 7974-7984
    • Claas, C.1    Stipp, C.S.2    Hemler, M.E.3
  • 14
    • 0035500912 scopus 로고    scopus 로고
    • PGRL is a major CD81-associated protein on lymphocytes and distinguishes a new family of cell surface proteins
    • K.L. Clark, Z. Zeng, A.L. Langford, S.M. Bowen, and S.C. Todd PGRL is a major CD81-associated protein on lymphocytes and distinguishes a new family of cell surface proteins Journal of Immunology 167 2001 5115 5121
    • (2001) Journal of Immunology , vol.167 , pp. 5115-5121
    • Clark, K.L.1    Zeng, Z.2    Langford, A.L.3    Bowen, S.M.4    Todd, S.C.5
  • 15
    • 67349207886 scopus 로고    scopus 로고
    • Mutation of juxtamembrane cysteines in the tetraspanin CD81 affects palmitoylation and alters interaction with other proteins at the cell surface
    • C. Delandre, T.R. Penabaz, A.L. Passarelli, S.K. Chapes, and R.J. Clem Mutation of juxtamembrane cysteines in the tetraspanin CD81 affects palmitoylation and alters interaction with other proteins at the cell surface Experimental Cell Research 315 2009 1953 1963
    • (2009) Experimental Cell Research , vol.315 , pp. 1953-1963
    • Delandre, C.1    Penabaz, T.R.2    Passarelli, A.L.3    Chapes, S.K.4    Clem, R.J.5
  • 17
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • M. Egeblad, and Z. Werb New functions for the matrix metalloproteinases in cancer progression Nature Reviews Cancer 2 2002 161 174
    • (2002) Nature Reviews Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 18
    • 0035816605 scopus 로고    scopus 로고
    • Functional interplay between type i collagen and cell surface matrix metalloproteinase activity
    • S.M. Ellerbroek, Y.I. Wu, C.M. Overall, and M.S. Stack Functional interplay between type I collagen and cell surface matrix metalloproteinase activity Journal of Biological Chemistry 276 2001 24833 24842
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 24833-24842
    • Ellerbroek, S.M.1    Wu, Y.I.2    Overall, C.M.3    Stack, M.S.4
  • 20
    • 77049111600 scopus 로고    scopus 로고
    • Emerging concepts in the regulation of membrane-type 1 matrix metalloproteinase activity
    • D. Gingras, and R. Beliveau Emerging concepts in the regulation of membrane-type 1 matrix metalloproteinase activity Biochimica et Biophysica Acta 1803 2010 142 150
    • (2010) Biochimica et Biophysica Acta , vol.1803 , pp. 142-150
    • Gingras, D.1    Beliveau, R.2
  • 21
    • 59849083832 scopus 로고    scopus 로고
    • Immunoglobulin superfamily member IgSF8 (EWI-2) and CD9 in fertilisation: Evidence of distinct functions for CD9 and a CD9-associated protein in mammalian sperm-egg interaction
    • A.I. Glazar, and J.P. Evans Immunoglobulin superfamily member IgSF8 (EWI-2) and CD9 in fertilisation: evidence of distinct functions for CD9 and a CD9-associated protein in mammalian sperm-egg interaction Reproduction, Fertility, and Development 21 2009 293 303
    • (2009) Reproduction, Fertility, and Development , vol.21 , pp. 293-303
    • Glazar, A.I.1    Evans, J.P.2
  • 22
    • 0028955867 scopus 로고
    • Biotinylation and assessment of membrane polarity: Caveats and methodological concerns
    • C.J. Gottardi, L.A. Dunbar, and M.J. Caplan Biotinylation and assessment of membrane polarity: caveats and methodological concerns American Journal of Physiology 268 1995 F285 F295
    • (1995) American Journal of Physiology , vol.268
    • Gottardi, C.J.1    Dunbar, L.A.2    Caplan, M.J.3
  • 23
    • 0344708475 scopus 로고    scopus 로고
    • Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain
    • M.E. Hemler Tetraspanin proteins mediate cellular penetration, invasion, and fusion events and define a novel type of membrane microdomain Annual Review of Cell and Developmental Biology 19 2003 397 422
    • (2003) Annual Review of Cell and Developmental Biology , vol.19 , pp. 397-422
    • Hemler, M.E.1
  • 24
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • M.E. Hemler Tetraspanin functions and associated microdomains Nature Reviews Molecular Cell Biology 6 2005 801 811
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 25
    • 0034697144 scopus 로고    scopus 로고
    • Binding of active (57 kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation
    • S. Hernandez-Barrantes, M. Toth, M.M. Bernardo, M. Yurkova, D.C. Gervasi, and Y. Raz Binding of active (57 kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation Journal of Biological Chemistry 275 2000 12080 12089
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 12080-12089
    • Hernandez-Barrantes, S.1    Toth, M.2    Bernardo, M.M.3    Yurkova, M.4    Gervasi, D.C.5    Raz, Y.6
  • 26
    • 79952468378 scopus 로고    scopus 로고
    • Functional analysis of bispecific antibody (EpCAMxCD3)-mediated T-lymphocyte and cancer cell interaction by single-cell force spectroscopy
    • S.C. Hoffmann, G.H. Wabnitz, Y. Samstag, G. Moldenhauer, and T. Ludwig Functional analysis of bispecific antibody (EpCAMxCD3)-mediated T-lymphocyte and cancer cell interaction by single-cell force spectroscopy International Journal of Cancer 128 2010 2096 2104
    • (2010) International Journal of Cancer , vol.128 , pp. 2096-2104
    • Hoffmann, S.C.1    Wabnitz, G.H.2    Samstag, Y.3    Moldenhauer, G.4    Ludwig, T.5
  • 27
    • 2142784516 scopus 로고    scopus 로고
    • MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover
    • K. Holmbeck, P. Bianco, J. Caterina, S. Yamada, M. Kromer, and S.A. Kuznetsov MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover Cell 99 1999 81 92
    • (1999) Cell , vol.99 , pp. 81-92
    • Holmbeck, K.1    Bianco, P.2    Caterina, J.3    Yamada, S.4    Kromer, M.5    Kuznetsov, S.A.6
  • 29
    • 49149106418 scopus 로고    scopus 로고
    • Dimerization of endogenous MT1-MMP is a regulatory step in the activation of the 72-kDa gelatinase MMP-2 on fibroblasts and fibrosarcoma cells
    • S. Ingvarsen, D.H. Madsen, T. Hillig, L.R. Lund, K. Holmbeck, and N. Behrendt Dimerization of endogenous MT1-MMP is a regulatory step in the activation of the 72-kDa gelatinase MMP-2 on fibroblasts and fibrosarcoma cells Biological Chemistry 389 2008 943 953
    • (2008) Biological Chemistry , vol.389 , pp. 943-953
    • Ingvarsen, S.1    Madsen, D.H.2    Hillig, T.3    Lund, L.R.4    Holmbeck, K.5    Behrendt, N.6
  • 30
    • 33749535260 scopus 로고    scopus 로고
    • MT1-MMP: A key regulator of cell migration in tissue
    • Y. Itoh MT1-MMP: a key regulator of cell migration in tissue IUBMB Life 58 2006 589 596
    • (2006) IUBMB Life , vol.58 , pp. 589-596
    • Itoh, Y.1
  • 31
    • 33845396458 scopus 로고    scopus 로고
    • Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP
    • Y. Itoh, N. Ito, H. Nagase, R.D. Evans, S.A. Bird, and M. Seiki Cell surface collagenolysis requires homodimerization of the membrane-bound collagenase MT1-MMP Molecular Biology of the Cell 17 2006 5390 5399
    • (2006) Molecular Biology of the Cell , vol.17 , pp. 5390-5399
    • Itoh, Y.1    Ito, N.2    Nagase, H.3    Evans, R.D.4    Bird, S.A.5    Seiki, M.6
  • 32
    • 45149126165 scopus 로고    scopus 로고
    • The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface
    • Y. Itoh, N. Ito, H. Nagase, and M. Seiki The second dimer interface of MT1-MMP, the transmembrane domain, is essential for ProMMP-2 activation on the cell surface Journal of Biological Chemistry 283 2008 13053 13062
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 13053-13062
    • Itoh, Y.1    Ito, N.2    Nagase, H.3    Seiki, M.4
  • 33
    • 3242772983 scopus 로고    scopus 로고
    • MT1-MMP: An enzyme with multidimensional regulation
    • Y. Itoh, and M. Seiki MT1-MMP: an enzyme with multidimensional regulation Trends in Biochemical Sciences 29 2004 285 289
    • (2004) Trends in Biochemical Sciences , vol.29 , pp. 285-289
    • Itoh, Y.1    Seiki, M.2
  • 36
    • 0028875824 scopus 로고
    • Cloning and characterization of MVP17: A developmentally regulated myelin protein in oligodendrocytes
    • T. Kim, K. Fiedler, D.L. Madison, W.H. Krueger, and S.E. Pfeiffer Cloning and characterization of MVP17: a developmentally regulated myelin protein in oligodendrocytes Journal of Neuroscience Research 42 1995 413 422
    • (1995) Journal of Neuroscience Research , vol.42 , pp. 413-422
    • Kim, T.1    Fiedler, K.2    Madison, D.L.3    Krueger, W.H.4    Pfeiffer, S.E.5
  • 37
    • 79957646416 scopus 로고    scopus 로고
    • Interdependency of cell adhesion, force generation and extracellular proteolysis in matrix remodeling
    • R. Kirmse, H. Otto, and T. Ludwig Interdependency of cell adhesion, force generation and extracellular proteolysis in matrix remodeling Journal of Cell Science 124 2011 1857 1866
    • (2011) Journal of Cell Science , vol.124 , pp. 1857-1866
    • Kirmse, R.1    Otto, H.2    Ludwig, T.3
  • 39
    • 0032583125 scopus 로고    scopus 로고
    • Integration of endothelial cells in multicellular spheroids prevents apoptosis and induces differentiation
    • T. Korff, and H.G. Augustin Integration of endothelial cells in multicellular spheroids prevents apoptosis and induces differentiation Journal of Cell Biology 143 1998 1341 1352
    • (1998) Journal of Cell Biology , vol.143 , pp. 1341-1352
    • Korff, T.1    Augustin, H.G.2
  • 40
    • 0035121532 scopus 로고    scopus 로고
    • Blood vessel maturation in a 3-dimensional spheroidal coculture model: Direct contact with smooth muscle cells regulates endothelial cell quiescence and abrogates VEGF responsiveness
    • T. Korff, S. Kimmina, G. Martiny-Baron, and H.G. Augustin Blood vessel maturation in a 3-dimensional spheroidal coculture model: direct contact with smooth muscle cells regulates endothelial cell quiescence and abrogates VEGF responsiveness FASEB Journal 15 2001 447 457
    • (2001) FASEB Journal , vol.15 , pp. 447-457
    • Korff, T.1    Kimmina, S.2    Martiny-Baron, G.3    Augustin, H.G.4
  • 41
    • 2942716714 scopus 로고    scopus 로고
    • Three-dimensional spheroidal culture of cytotrophoblast cells mimics the phenotype and differentiation of cytotrophoblasts from normal and preeclamptic pregnancies
    • T. Korff, T. Krauss, and H.G. Augustin Three-dimensional spheroidal culture of cytotrophoblast cells mimics the phenotype and differentiation of cytotrophoblasts from normal and preeclamptic pregnancies Experimental Cell Research 297 2004 415 423
    • (2004) Experimental Cell Research , vol.297 , pp. 415-423
    • Korff, T.1    Krauss, T.2    Augustin, H.G.3
  • 42
    • 0942279501 scopus 로고    scopus 로고
    • Evidence for specific tetraspanin homodimers: Inhibition of palmitoylation makes cysteine residues available for cross-linking
    • O.V. Kovalenko, X. Yang, T.V. Kolesnikova, and M.E. Hemler Evidence for specific tetraspanin homodimers: inhibition of palmitoylation makes cysteine residues available for cross-linking Biochemical Journal 377 2004 407 417
    • (2004) Biochemical Journal , vol.377 , pp. 407-417
    • Kovalenko, O.V.1    Yang, X.2    Kolesnikova, T.V.3    Hemler, M.E.4
  • 43
    • 65249142254 scopus 로고    scopus 로고
    • Tetraspanin proteins regulate membrane type-1 matrix metalloproteinase (MT1-MMP)-dependent pericellular proteolysis
    • M. Lafleur, D. Xu, and M.E. Hemler Tetraspanin proteins regulate membrane type-1 matrix metalloproteinase (MT1-MMP)-dependent pericellular proteolysis Molecular Biology of the Cell 20 2009 2030 2040
    • (2009) Molecular Biology of the Cell , vol.20 , pp. 2030-2040
    • Lafleur, M.1    Xu, D.2    Hemler, M.E.3
  • 44
    • 33845975257 scopus 로고    scopus 로고
    • Membrane microdomains and proteomics: Lessons from tetraspanin microdomains and comparison with lipid rafts
    • F. Le Naour, M. Andre, C. Boucheix, and E. Rubinstein Membrane microdomains and proteomics: lessons from tetraspanin microdomains and comparison with lipid rafts Proteomics 6 2006 6447 6454
    • (2006) Proteomics , vol.6 , pp. 6447-6454
    • Le Naour, F.1    Andre, M.2    Boucheix, C.3    Rubinstein, E.4
  • 46
    • 24044439517 scopus 로고    scopus 로고
    • Protein-protein interactions in the tetraspanin web
    • S. Levy, and T. Shoham Protein-protein interactions in the tetraspanin web Physiology (Bethesda) 20 2005 218 224
    • (2005) Physiology (Bethesda) , vol.20 , pp. 218-224
    • Levy, S.1    Shoham, T.2
  • 47
    • 13444259476 scopus 로고    scopus 로고
    • The tetraspanin web modulates immune-signalling complexes
    • S. Levy, and T. Shoham The tetraspanin web modulates immune-signalling complexes Nature Reviews Immunology 5 2005 136 148
    • (2005) Nature Reviews Immunology , vol.5 , pp. 136-148
    • Levy, S.1    Shoham, T.2
  • 48
    • 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
    • K.D. Little, M.E. Hemler, and C.S. Stipp Dynamic regulation of a GPCR-tetraspanin-G protein complex on intact cells: central role of CD81 in facilitating GPR56-Galpha q/11 association Molecular Biology of the Cell 15 2004 2375 2387
    • (2004) Molecular Biology of the Cell , vol.15 , pp. 2375-2387
    • Little, K.D.1    Hemler, M.E.2    Stipp, C.S.3
  • 49
    • 30444432840 scopus 로고    scopus 로고
    • Local proteolytic activity in tumor cell invasion and metastasis
    • T. Ludwig Local proteolytic activity in tumor cell invasion and metastasis Bioessays 27 2005 1181 1191
    • (2005) Bioessays , vol.27 , pp. 1181-1191
    • Ludwig, T.1
  • 50
    • 43149103881 scopus 로고    scopus 로고
    • Probing cellular microenvironments and tissue remodeling by atomic force microscopy
    • T. Ludwig, R. Kirmse, K. Poole, and U.S. Schwarz Probing cellular microenvironments and tissue remodeling by atomic force microscopy Pflugers Archiv 456 2008 29 49
    • (2008) Pflugers Archiv , vol.456 , pp. 29-49
    • Ludwig, T.1    Kirmse, R.2    Poole, K.3    Schwarz, U.S.4
  • 51
    • 58149093961 scopus 로고    scopus 로고
    • The cytoplasmic tail dileucine motif LL572 determines the glycosylation pattern of membrane-type 1 matrix metalloproteinase
    • T. Ludwig, S.M. Theissen, M.J. Morton, and M.J. Caplan The cytoplasmic tail dileucine motif LL572 determines the glycosylation pattern of membrane-type 1 matrix metalloproteinase Journal of Biological Chemistry 283 2008 35410 35418
    • (2008) Journal of Biological Chemistry , vol.283 , pp. 35410-35418
    • Ludwig, T.1    Theissen, S.M.2    Morton, M.J.3    Caplan, M.J.4
  • 52
    • 0030947554 scopus 로고    scopus 로고
    • The tetraspanin superfamily: Molecular facilitators
    • H.T. Maecker, S.C. Todd, and S. Levy The tetraspanin superfamily: molecular facilitators FASEB Journal 11 1997 428 442
    • (1997) FASEB Journal , vol.11 , pp. 428-442
    • Maecker, H.T.1    Todd, S.C.2    Levy, S.3
  • 53
    • 70849100053 scopus 로고    scopus 로고
    • Membrane type-1 matrix metalloproteinase activity is regulated by the endocytic collagen receptor Endo180
    • G. Messaritou, L. East, C. Roghi, C.M. Isacke, and H. Yarwood Membrane type-1 matrix metalloproteinase activity is regulated by the endocytic collagen receptor Endo180 Journal of Cell Science 122 2009 4042 4048
    • (2009) Journal of Cell Science , vol.122 , pp. 4042-4048
    • Messaritou, G.1    East, L.2    Roghi, C.3    Isacke, C.M.4    Yarwood, H.5
  • 56
    • 2642546699 scopus 로고    scopus 로고
    • Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP)
    • P. Osenkowski, M. Toth, and R. Fridman Processing, shedding, and endocytosis of membrane type 1-matrix metalloproteinase (MT1-MMP) Journal of Cellular Physiology 200 2004 2 10
    • (2004) Journal of Cellular Physiology , vol.200 , pp. 2-10
    • Osenkowski, P.1    Toth, M.2    Fridman, R.3
  • 57
    • 70350417461 scopus 로고    scopus 로고
    • Matrix invasion by tumour cells: A focus on MT1-MMP trafficking to invadopodia
    • R. Poincloux, F. Lizarraga, and P. Chavrier Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia Journal of Cell Science 122 2009 3015 3024
    • (2009) Journal of Cell Science , vol.122 , pp. 3015-3024
    • Poincloux, R.1    Lizarraga, F.2    Chavrier, P.3
  • 59
    • 0032500602 scopus 로고    scopus 로고
    • Tyrosine-based membrane protein sorting signals are differentially interpreted by polarized Madin-Darby canine kidney and LLC-PK1 epithelial cells
    • D.L. Roush, C.J. Gottardi, H.Y. Naim, M.G. Roth, and M.J. Caplan Tyrosine-based membrane protein sorting signals are differentially interpreted by polarized Madin-Darby canine kidney and LLC-PK1 epithelial cells Journal of Biological Chemistry 273 1998 26862 26869
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 26862-26869
    • Roush, D.L.1    Gottardi, C.J.2    Naim, H.Y.3    Roth, M.G.4    Caplan, M.J.5
  • 60
    • 77957281923 scopus 로고    scopus 로고
    • Coordinate action of membrane-type matrix metalloproteinase -1 (MT1-MMP) and MMP-2 enhances pericellular proteolysis and invasion
    • H. Sato, and T. Takino Coordinate action of membrane-type matrix metalloproteinase -1 (MT1-MMP) and MMP-2 enhances pericellular proteolysis and invasion Cancer Sci 101 2010 843 847
    • (2010) Cancer Sci , vol.101 , pp. 843-847
    • Sato, H.1    Takino, T.2
  • 61
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • H. Sato, T. Takino, Y. Okada, J. Cao, A. Shinagawa, and E. Yamamoto A matrix metalloproteinase expressed on the surface of invasive tumour cells Nature 370 1994 61 65
    • (1994) Nature , vol.370 , pp. 61-65
    • Sato, H.1    Takino, T.2    Okada, Y.3    Cao, J.4    Shinagawa, A.5    Yamamoto, E.6
  • 63
    • 32044459101 scopus 로고    scopus 로고
    • Building of the tetraspanin web: Distinct structural domains of CD81 function in different cellular compartments
    • T. Shoham, R. Rajapaksa, C.-C. Kuo, J. Haimovich, and S. Levy Building of the tetraspanin web: distinct structural domains of CD81 function in different cellular compartments Molecular and Cellular Biology 26 2006 1373 1385
    • (2006) Molecular and Cellular Biology , vol.26 , pp. 1373-1385
    • Shoham, T.1    Rajapaksa, R.2    Kuo, C.-C.3    Haimovich, J.4    Levy, S.5
  • 64
    • 0035798537 scopus 로고    scopus 로고
    • EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
    • C.S. Stipp, T.V. Kolesnikova, and M.E. Hemler EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily Journal of Biological Chemistry 276 2001 40545 40554
    • (2001) Journal of Biological Chemistry , vol.276 , pp. 40545-40554
    • Stipp, C.S.1    Kolesnikova, T.V.2    Hemler, M.E.3
  • 65
    • 0346849708 scopus 로고    scopus 로고
    • EWI-2 regulates alpha3beta1 integrin-dependent cell functions on laminin-5
    • C.S. Stipp, T.V. Kolesnikova, and M.E. Hemler EWI-2 regulates alpha3beta1 integrin-dependent cell functions on laminin-5 Journal of Cell Biology 163 2003 1167 1177
    • (2003) Journal of Cell Biology , vol.163 , pp. 1167-1177
    • Stipp, C.S.1    Kolesnikova, T.V.2    Hemler, M.E.3
  • 68
    • 0037135611 scopus 로고    scopus 로고
    • Complex pattern of membrane type 1 matrix metalloproteinase shedding. Regulation by autocatalytic cells surface inactivation of active enzyme
    • M. Toth, S. Hernandez-Barrantes, P. Osenkowski, M.M. Bernardo, D.C. Gervasi, and Y. Shimura Complex pattern of membrane type 1 matrix metalloproteinase shedding. Regulation by autocatalytic cells surface inactivation of active enzyme Journal of Biological Chemistry 277 2002 26340 26350
    • (2002) Journal of Biological Chemistry , vol.277 , pp. 26340-26350
    • Toth, M.1    Hernandez-Barrantes, S.2    Osenkowski, P.3    Bernardo, M.M.4    Gervasi, D.C.5    Shimura, Y.6
  • 69
    • 0036911337 scopus 로고    scopus 로고
    • Specific heterodimer formation is a prerequisite for uroplakins to exit from the endoplasmic reticulum
    • L. Tu, T.T. Sun, and G. Kreibich Specific heterodimer formation is a prerequisite for uroplakins to exit from the endoplasmic reticulum Molecular Biology of the Cell 13 2002 4221 4230
    • (2002) Molecular Biology of the Cell , vol.13 , pp. 4221-4230
    • Tu, L.1    Sun, T.T.2    Kreibich, G.3
  • 70
    • 0035945354 scopus 로고    scopus 로고
    • Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity
    • T. Uekita, Y. Itoh, I. Yana, H. Ohno, and M. Seiki Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity Journal of Cell Biology 155 2001 1345 1356
    • (2001) Journal of Cell Biology , vol.155 , pp. 1345-1356
    • Uekita, T.1    Itoh, Y.2    Yana, I.3    Ohno, H.4    Seiki, M.5
  • 71
    • 79961142381 scopus 로고    scopus 로고
    • The C-terminal tail of tetraspanin protein CD9 contributes to its function and molecular organization
    • H.-X. Wang, T.V. Kolesnikova, C. Denison, S.P. Gygi, and M.E. Hemler The C-terminal tail of tetraspanin protein CD9 contributes to its function and molecular organization Journal of Cell Science 124 2011 2702 2710
    • (2011) Journal of Cell Science , vol.124 , pp. 2702-2710
    • Wang, H.-X.1    Kolesnikova, T.V.2    Denison, C.3    Gygi, S.P.4    Hemler, M.E.5
  • 72
  • 73
    • 54049111439 scopus 로고    scopus 로고
    • MT1-MMP collagenolytic activity is regulated through association with tetraspanin CD151 in primary endothelial cells
    • M. Yanez-Mo, O. Barreiro, P. Gonzalo, A. Batista, D. Megias, and L. Genis MT1-MMP collagenolytic activity is regulated through association with tetraspanin CD151 in primary endothelial cells Blood 112 2008 3217 3226
    • (2008) Blood , vol.112 , pp. 3217-3226
    • Yanez-Mo, M.1    Barreiro, O.2    Gonzalo, P.3    Batista, A.4    Megias, D.5    Genis, L.6
  • 75
    • 0036198534 scopus 로고    scopus 로고
    • Palmitoylation of tetraspanin proteins: Modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology
    • X. Yang, C. Claas, S.K. Kraeft, L.B. Chen, Z. Wang, and J.A. Kreidberg Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology Molecular Biology of the Cell 13 2002 767 781
    • (2002) Molecular Biology of the 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
  • 77
    • 0038179866 scopus 로고    scopus 로고
    • EWI2/PGRL associates with the metastasis suppressor KAI1/CD82 and inhibits the migration of prostate cancer cells
    • X.A. Zhang, W.S. Lane, S. Charrin, E. Rubinstein, and L. Liu EWI2/PGRL associates with the metastasis suppressor KAI1/CD82 and inhibits the migration of prostate cancer cells Cancer Research 63 2003 2665 2674
    • (2003) Cancer Research , vol.63 , pp. 2665-2674
    • Zhang, X.A.1    Lane, W.S.2    Charrin, S.3    Rubinstein, E.4    Liu, L.5
  • 78
    • 0036901565 scopus 로고    scopus 로고
    • Rapid trafficking of membrane type 1-matrix metalloproteinase to the cell surface regulates progelatinase a activation
    • S. Zucker, M. Hymowitz, C.E. Conner, E.A. DiYanni, and J. Cao Rapid trafficking of membrane type 1-matrix metalloproteinase to the cell surface regulates progelatinase a activation Laboratory Investigation 82 2002 1673 1684
    • (2002) Laboratory Investigation , vol.82 , pp. 1673-1684
    • Zucker, S.1    Hymowitz, M.2    Conner, C.E.3    Diyanni, E.A.4    Cao, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.