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Volumn 20, Issue 10, 2015, Pages 847-859

MT1-MMP recognition by ERM proteins and its implication in CD44 shedding

Author keywords

[No Author keywords available]

Indexed keywords

EZRIN RADIXIN MOESIN PROTEIN; F ACTIN; HERMES ANTIGEN; MATRIX METALLOPROTEINASE 14; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; ACTIN; CD44 PROTEIN, HUMAN; CYTOSKELETON PROTEIN; DNA BINDING PROTEIN; ETV5 PROTEIN, HUMAN; MMP14 PROTEIN, HUMAN; PROTEIN BINDING; RADIXIN; TRANSCRIPTION FACTOR;

EID: 84943347613     PISSN: 13569597     EISSN: 13652443     Source Type: Journal    
DOI: 10.1111/gtc.12276     Document Type: Article
Times cited : (23)

References (58)
  • 1
    • 80053642374 scopus 로고    scopus 로고
    • The Phenix software for automated determination of macromolecular structures
    • Adams, P.D., Afonine, P.V., Bunkóczi, G. et al. (2011) The Phenix software for automated determination of macromolecular structures. Methods 55, 94-106.
    • (2011) Methods , vol.55 , pp. 94-106
    • Adams, P.D.1    Afonine, P.V.2    Bunkóczi, G.3
  • 2
    • 23444460823 scopus 로고    scopus 로고
    • Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration
    • Anilkumar, N., Uekita, T., Couchman, J.R., Nagase, H., Seiki, M. & Itoh, Y. (2005) Palmitoylation at Cys574 is essential for MT1-MMP to promote cell migration. FASEB J. 19, 1326-1328.
    • (2005) FASEB J. , vol.19 , pp. 1326-1328
    • Anilkumar, N.1    Uekita, T.2    Couchman, J.R.3    Nagase, H.4    Seiki, M.5    Itoh, Y.6
  • 3
    • 33645507413 scopus 로고    scopus 로고
    • Dynamic interactions of cortactin and membrane type 1 matrix metalloproteinase at invadopodia: defining the stages of invadopodia formation and function
    • Artym, V.V., Zhang, Y., Seillier-Moiseiwitsch, F., Yamada, K.M. & Mueller, S.C. (2006) Dynamic interactions of cortactin and membrane type 1 matrix metalloproteinase at invadopodia: defining the stages of invadopodia formation and function. Cancer Res. 66, 3034-3043.
    • (2006) Cancer Res. , vol.66 , pp. 3034-3043
    • Artym, V.V.1    Zhang, Y.2    Seillier-Moiseiwitsch, F.3    Yamada, K.M.4    Mueller, S.C.5
  • 4
    • 0034194447 scopus 로고    scopus 로고
    • Molecular organization, structural features, and ligand binding characteristics of CD44, a highly variable cell surface glycoprotein with multiple functions
    • Bajorath, J. (2000) Molecular organization, structural features, and ligand binding characteristics of CD44, a highly variable cell surface glycoprotein with multiple functions. Proteins 39, 103-111.
    • (2000) Proteins , vol.39 , pp. 103-111
    • Bajorath, J.1
  • 5
  • 6
    • 1842790801 scopus 로고    scopus 로고
    • Distinct roles for the catalytic and hemopexin domains of membrane type 1-matrix metalloproteinase in substrate degradation and cell migration
    • Cao, J., Kozarekar, P., Pavlaki, M., Chiarelli, C., Bahou, W.F. & Zucker, S. (2004) Distinct roles for the catalytic and hemopexin domains of membrane type 1-matrix metalloproteinase in substrate degradation and cell migration. J. Biol. Chem. 279, 14129-14139.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14129-14139
    • Cao, J.1    Kozarekar, P.2    Pavlaki, M.3    Chiarelli, C.4    Bahou, W.F.5    Zucker, S.6
  • 9
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad, M. & Werb, Z. (2002) New functions for the matrix metalloproteinases in cancer progression. Nat. Rev. Cancer 2, 161-174.
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 12
    • 84869138409 scopus 로고    scopus 로고
    • Structural basis of the junctional anchorage of the cerebral cavernous malformations complex
    • Gingras, A.R., Liu, J.J. & Ginsberg, M.H. (2012) Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. J. Cell Biol. 199, 39-48.
    • (2012) J. Cell Biol. , vol.199 , pp. 39-48
    • Gingras, A.R.1    Liu, J.J.2    Ginsberg, M.H.3
  • 13
    • 77049111600 scopus 로고    scopus 로고
    • Emerging concepts in the regulation of membrane-type 1 matrix metalloproteinase activity
    • Gingras, D. & Béliveau, R. (2010) Emerging concepts in the regulation of membrane-type 1 matrix metalloproteinase activity. Biochim. Biophys. Acta 1803, 142-150.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 142-150
    • Gingras, D.1    Béliveau, R.2
  • 14
    • 0035955469 scopus 로고    scopus 로고
    • Activation of the extracellular signal-regulated protein kinase (ERK) cascade by membrane-type-1 matrix metalloproteinase (MT1-MMP)
    • Gingras, D., Bousquet-Gagnon, N., Langlois, S., Lachambre, M.P., Annabi, B. & Béliveau, R. (2001) Activation of the extracellular signal-regulated protein kinase (ERK) cascade by membrane-type-1 matrix metalloproteinase (MT1-MMP). FEBS Lett. 507, 231-236.
    • (2001) FEBS Lett. , vol.507 , pp. 231-236
    • Gingras, D.1    Bousquet-Gagnon, N.2    Langlois, S.3    Lachambre, M.P.4    Annabi, B.5    Béliveau, R.6
  • 15
    • 38649103149 scopus 로고    scopus 로고
    • Sphingosine-1-phosphate induces the association of membrane-type 1 matrix metalloproteinase with p130Cas in endothelial cells
    • Gingras, D., Michaud, M., Di Tomasso, G., Béliveau, E., Nyalendo, C. & Béliveau, R. (2008) Sphingosine-1-phosphate induces the association of membrane-type 1 matrix metalloproteinase with p130Cas in endothelial cells. FEBS Lett. 582, 399-404.
    • (2008) FEBS Lett. , vol.582 , pp. 399-404
    • Gingras, D.1    Michaud, M.2    Di Tomasso, G.3    Béliveau, E.4    Nyalendo, C.5    Béliveau, R.6
  • 17
    • 0034283003 scopus 로고    scopus 로고
    • Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain
    • Hamada, K., Shimizu, T., Matsui, T., Tsukita, S. & Hakoshima, T. (2000b) Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. EMBO J. 19, 4449-4462.
    • (2000) EMBO J. , vol.19 , pp. 4449-4462
    • Hamada, K.1    Shimizu, T.2    Matsui, T.3    Tsukita, S.4    Hakoshima, T.5
  • 18
    • 0037415682 scopus 로고    scopus 로고
    • Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex
    • Hamada, K., Shimizu, T., Yonemura, S., Tsukita, S., Tsukita, S. & Hakoshima, T. (2003) Structural basis of adhesion-molecule recognition by ERM proteins revealed by the crystal structure of the radixin-ICAM-2 complex. EMBO J. 22, 502-514.
    • (2003) EMBO J. , vol.22 , pp. 502-514
    • Hamada, K.1    Shimizu, T.2    Yonemura, S.3    Tsukita, S.4    Tsukita, S.5    Hakoshima, T.6
  • 19
    • 0346365374 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases in the microenvironment of spontaneous and experimental melanoma metastases reflects the requirements for tumor formation
    • Hofmann, U.B., Eggert, A.A.O., Blass, K., Bröcker, E.-B. & Becker, J.C. (2003) Expression of matrix metalloproteinases in the microenvironment of spontaneous and experimental melanoma metastases reflects the requirements for tumor formation. Cancer Res. 63, 8221-8225.
    • (2003) Cancer Res. , vol.63 , pp. 8221-8225
    • Hofmann, U.B.1    Eggert, A.A.O.2    Blass, K.3    Bröcker, E.-B.4    Becker, J.C.5
  • 21
    • 0035801473 scopus 로고    scopus 로고
    • Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion
    • Itoh, Y., Takamura, A., Ito, N., Maru, Y., Sato, H., Suenaga, N., Aoki, T. & Seiki, M. (2001) Homophilic complex formation of MT1-MMP facilitates proMMP-2 activation on the cell surface and promotes tumor cell invasion. EMBO J. 20, 4782-4793.
    • (2001) EMBO J. , vol.20 , pp. 4782-4793
    • Itoh, Y.1    Takamura, A.2    Ito, N.3    Maru, Y.4    Sato, H.5    Suenaga, N.6    Aoki, T.7    Seiki, M.8
  • 22
    • 0035947766 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration
    • Kajita, M., Itoh, Y., Chiba, T., Mori, H., Okada, A., Kinoh, H. & Seiki, M. (2001) Membrane-type 1 matrix metalloproteinase cleaves CD44 and promotes cell migration. J. Cell Biol. 153, 893-904.
    • (2001) J. Cell Biol. , vol.153 , pp. 893-904
    • Kajita, M.1    Itoh, Y.2    Chiba, T.3    Mori, H.4    Okada, A.5    Kinoh, H.6    Seiki, M.7
  • 23
    • 10644229956 scopus 로고    scopus 로고
    • Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase
    • Labrecque, L., Nyalendo, C., Langlois, S., Durocher, Y., Roghi, C., Murphy, G., Gingras, D. & Béliveau, R. (2004) Src-mediated tyrosine phosphorylation of caveolin-1 induces its association with membrane type 1 matrix metalloproteinase. J. Biol. Chem. 279, 52132-52140.
    • (2004) J. Biol. Chem. , vol.279 , pp. 52132-52140
    • Labrecque, L.1    Nyalendo, C.2    Langlois, S.3    Durocher, Y.4    Roghi, C.5    Murphy, G.6    Gingras, D.7    Béliveau, R.8
  • 24
    • 1842474897 scopus 로고    scopus 로고
    • Membrane type 1-matrix metalloproteinase (MT1-MMP) cooperates with sphingosine 1-phosphate to induce endothelial cell migration and morphogenic differentiation
    • Langlois, S., Gingras, D. & Béliveau, R. (2004) Membrane type 1-matrix metalloproteinase (MT1-MMP) cooperates with sphingosine 1-phosphate to induce endothelial cell migration and morphogenic differentiation. Blood 103, 3020-3028.
    • (2004) Blood , vol.103 , pp. 3020-3028
    • Langlois, S.1    Gingras, D.2    Béliveau, R.3
  • 25
    • 0034685778 scopus 로고    scopus 로고
    • Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain
    • Lehti, K., Valtanen, H., Wickström, S.A., Lohi, J. & Keski-Oja, J. (2000) Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain. J. Biol. Chem. 275, 15006-15013.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15006-15013
    • Lehti, K.1    Valtanen, H.2    Wickström, S.A.3    Lohi, J.4    Keski-Oja, J.5
  • 26
    • 0027491845 scopus 로고
    • CD44 and its interaction with extracellular matrix
    • Lesley, J., Hyman, R. & Kincade, P.W. (1993) CD44 and its interaction with extracellular matrix. Adv. Immunol. 54, 271-335.
    • (1993) Adv. Immunol. , vol.54 , pp. 271-335
    • Lesley, J.1    Hyman, R.2    Kincade, P.W.3
  • 28
    • 84862690469 scopus 로고    scopus 로고
    • Structural basis for small G protein effector interaction of Ras-related protein 1 (Rap1) and adaptor protein Krev interaction trapped 1 (KRIT1)
    • Li, X., Zhang, R., Draheim, K.M., Liu, W., Calderwood, D.A. & Boggon, T.J. (2012) Structural basis for small G protein effector interaction of Ras-related protein 1 (Rap1) and adaptor protein Krev interaction trapped 1 (KRIT1). J. Biol. Chem. 287, 22317-22327.
    • (2012) J. Biol. Chem. , vol.287 , pp. 22317-22327
    • Li, X.1    Zhang, R.2    Draheim, K.M.3    Liu, W.4    Calderwood, D.A.5    Boggon, T.J.6
  • 29
    • 54049102110 scopus 로고    scopus 로고
    • Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase
    • Li, X.-Y., Ota, I., Yana, I., Sabeh, F. & Weiss, S.J. (2008) Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase. Mol. Biol. Cell 19, 3221-3233.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3221-3233
    • Li, X.-Y.1    Ota, I.2    Yana, I.3    Sabeh, F.4    Weiss, S.J.5
  • 30
    • 34250026140 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of focal adhesion kinase
    • Lietha, D., Cai, X., Ceccarelli, D.F., Li, Y., Schaller, M.D. & Eck, M.J. (2007) Structural basis for the autoinhibition of focal adhesion kinase. Cell 129, 1177-1187.
    • (2007) Cell , vol.129 , pp. 1177-1187
    • Lietha, D.1    Cai, X.2    Ceccarelli, D.F.3    Li, Y.4    Schaller, M.D.5    Eck, M.J.6
  • 33
    • 0036683241 scopus 로고    scopus 로고
    • CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain
    • Mori, H., Tomari, T., Koshikawa, N., Kajita, M., Itoh, Y., Sato, H., Tojo, H., Yana, I. & Seiki, M. (2002) CD44 directs membrane-type 1 matrix metalloproteinase to lamellipodia by associating with its hemopexin-like domain. EMBO J. 21, 3949-3959.
    • (2002) EMBO J. , vol.21 , pp. 3949-3959
    • Mori, H.1    Tomari, T.2    Koshikawa, N.3    Kajita, M.4    Itoh, Y.5    Sato, H.6    Tojo, H.7    Yana, I.8    Seiki, M.9
  • 35
    • 0030791315 scopus 로고    scopus 로고
    • Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion
    • Nakahara, H., Howard, L., Thompson, E.W., Sato, H., Seiki, M., Yeh, Y. & Chen, W.T. (1997) Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion. Proc. Natl Acad. Sci. USA 94, 7959-7964.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7959-7964
    • Nakahara, H.1    Howard, L.2    Thompson, E.W.3    Sato, H.4    Seiki, M.5    Yeh, Y.6    Chen, W.T.7
  • 36
    • 34447522132 scopus 로고    scopus 로고
    • Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration
    • Nyalendo, C., Michaud, M., Beaulieu, E., Roghi, C., Murphy, G., Gingras, D. & Béliveau, R. (2007) Src-dependent phosphorylation of membrane type I matrix metalloproteinase on cytoplasmic tyrosine 573: role in endothelial and tumor cell migration. J. Biol. Chem. 282, 15690-15699.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15690-15699
    • Nyalendo, C.1    Michaud, M.2    Beaulieu, E.3    Roghi, C.4    Murphy, G.5    Gingras, D.6    Béliveau, R.7
  • 37
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data
    • Otwinowski, Z. & Minor, W. (1997) Processing of X-ray diffraction data. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 33646576168 scopus 로고    scopus 로고
    • Degradomics: systems biology of the protease web. Pleiotropic roles of MMPs in cancer
    • Overall, C.M. & Dean, R.A. (2006) Degradomics: systems biology of the protease web. Pleiotropic roles of MMPs in cancer. Cancer Metastasis Rev. 25, 69-75.
    • (2006) Cancer Metastasis Rev. , vol.25 , pp. 69-75
    • Overall, C.M.1    Dean, R.A.2
  • 39
    • 0032514874 scopus 로고    scopus 로고
    • A structural explanation for the recognition of tyrosine-based endocytotic signals
    • Owen, D.J. & Evans, P.R. (1998) A structural explanation for the recognition of tyrosine-based endocytotic signals. Science 282, 1327-1332.
    • (1998) Science , vol.282 , pp. 1327-1332
    • Owen, D.J.1    Evans, P.R.2
  • 40
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw, A., Ewald, A.J. & Werb, Z. (2007) Matrix metalloproteinases and the regulation of tissue remodelling. Nat. Rev. Mol. Cell Biol. 8, 21-233.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 21-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 41
    • 70350417461 scopus 로고    scopus 로고
    • Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia
    • Poincloux, R., Lizárraga, F. & Chavrier, P. (2009) Matrix invasion by tumour cells: a focus on MT1-MMP trafficking to invadopodia. J. Cell Sci. 122, 3015-3024.
    • (2009) J. Cell Sci. , vol.122 , pp. 3015-3024
    • Poincloux, R.1    Lizárraga, F.2    Chavrier, P.3
  • 43
    • 65449123485 scopus 로고    scopus 로고
    • Cytoplasmic tail of MT1-MMP regulates macrophage motility independently from its protease activity
    • Sakamoto, T. & Seiki, M. (2009) Cytoplasmic tail of MT1-MMP regulates macrophage motility independently from its protease activity. Genes Cells 14, 617-626.
    • (2009) Genes Cells , vol.14 , pp. 617-626
    • Sakamoto, T.1    Seiki, M.2
  • 44
    • 0028291737 scopus 로고
    • A matrix metalloproteinase expressed on the surface of invasive tumour cells
    • Sato, H., Takino, T., Okada, Y., Cao, J., Shinagawa, A., Yamamoto, E. & Seiki, M. (1994) A matrix metalloproteinase expressed on the surface of invasive tumour cells. Nature 370, 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    Seiki, M.7
  • 46
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht, M.D. & Werb, Z. (2001) How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol. 17, 463-516.
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 47
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin, A.Y., Collier, I., Bannikov, G., Marmer, B.L., Grant, G.A. & Goldberg, G.I. (1995) Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J. Biol. Chem. 270, 5331-5338.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 48
    • 13444273084 scopus 로고    scopus 로고
    • CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase
    • Suenaga, N., Mori, H., Itoh, Y. & Seiki, M. (2005) CD44 binding through the hemopexin-like domain is critical for its shedding by membrane-type 1 matrix metalloproteinase. Oncogene 24, 859-868.
    • (2005) Oncogene , vol.24 , pp. 859-868
    • Suenaga, N.1    Mori, H.2    Itoh, Y.3    Seiki, M.4
  • 50
    • 47849118480 scopus 로고    scopus 로고
    • Structural basis of the cytoplasmic tail of adhesion molecule CD43 and its binding to ERM proteins
    • Takai, Y., Kitano, K., Terawaki, S., Maesaki, R. & Hakoshima, T. (2008) Structural basis of the cytoplasmic tail of adhesion molecule CD43 and its binding to ERM proteins. J. Mol. Biol. 381, 634-644.
    • (2008) J. Mol. Biol. , vol.381 , pp. 634-644
    • Takai, Y.1    Kitano, K.2    Terawaki, S.3    Maesaki, R.4    Hakoshima, T.5
  • 51
    • 53749103646 scopus 로고    scopus 로고
    • Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of membrane-type 1 matrix metalloproteinase (MT1-MMP)
    • Terawaki, S., Kitano, K., Aoyama, M. & Hakoshima, T. (2008) Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of membrane-type 1 matrix metalloproteinase (MT1-MMP). Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 64, 911-913.
    • (2008) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.64 , pp. 911-913
    • Terawaki, S.1    Kitano, K.2    Aoyama, M.3    Hakoshima, T.4
  • 52
    • 34547113109 scopus 로고    scopus 로고
    • Structural basis for type II membrane protein binding by ERM proteins revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex
    • Terawaki, S., Kitano, K. & Hakoshima, T. (2007) Structural basis for type II membrane protein binding by ERM proteins revealed by the radixin-neutral endopeptidase 24.11 (NEP) complex. J. Biol. Chem. 282, 19854-19862.
    • (2007) J. Biol. Chem. , vol.282 , pp. 19854-19862
    • Terawaki, S.1    Kitano, K.2    Hakoshima, T.3
  • 53
    • 33645992471 scopus 로고    scopus 로고
    • Structural basis for NHERF recognition by ERM proteins
    • Terawaki, S., Maesaki, R. & Hakoshima, T. (2006) Structural basis for NHERF recognition by ERM proteins. Structure 14, 777-789.
    • (2006) Structure , vol.14 , pp. 777-789
    • Terawaki, S.1    Maesaki, R.2    Hakoshima, T.3
  • 54
    • 0035945354 scopus 로고    scopus 로고
    • Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity
    • Uekita, T., Itoh, Y., Yana, I., Ohno, H. & Seiki, M. (2001) Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity. J. Cell Biol. 155, 1345-1356.
    • (2001) J. Cell Biol. , vol.155 , pp. 1345-1356
    • Uekita, T.1    Itoh, Y.2    Yana, I.3    Ohno, H.4    Seiki, M.5
  • 55
    • 0030951910 scopus 로고    scopus 로고
    • Expression and tissue localization of membrane-types 1, 2, and 3 matrix metalloproteinases in human invasive breast carcinomas
    • Ueno, H., Nakamura, H., Inoue, M., Imai, K., Noguchi, M., Sato, H., Seiki, M. & Okada, Y. (1997) Expression and tissue localization of membrane-types 1, 2, and 3 matrix metalloproteinases in human invasive breast carcinomas. Cancer Res. 57, 2055-2060.
    • (1997) Cancer Res. , vol.57 , pp. 2055-2060
    • Ueno, H.1    Nakamura, H.2    Inoue, M.3    Imai, K.4    Noguchi, M.5    Sato, H.6    Seiki, M.7    Okada, Y.8
  • 56
    • 0037693895 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry
    • Visse, R. & Nagase, H. (2003) Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ. Res. 92, 827-839.
    • (2003) Circ. Res. , vol.92 , pp. 827-839
    • Visse, R.1    Nagase, H.2
  • 57
    • 84869124279 scopus 로고    scopus 로고
    • N-WASP coordinates the delivery and F-actin-mediated capture of MT1-MMP at invasive pseudopods
    • Yu, X., Zech, T., McDonald, L. et al. (2012) N-WASP coordinates the delivery and F-actin-mediated capture of MT1-MMP at invasive pseudopods. J. Cell Biol. 199, 527-544.
    • (2012) J. Cell Biol. , vol.199 , pp. 527-544
    • Yu, X.1    Zech, T.2    McDonald, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.