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Volumn 9, Issue 2, 2005, Pages 185-196

FAK-Mediated Src phosphorylation of endophilin A2 inhibits endocytosis of MT1-MMP and promotes ECM degradation

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE PROTEIN; DYNAMIN; ENDOPHILIN; FOCAL ADHESION KINASE; MATRIX METALLOPROTEINASE 14; PROTEIN TYROSINE KINASE;

EID: 22944438407     PISSN: 15345807     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.devcel.2005.06.006     Document Type: Article
Times cited : (155)

References (41)
  • 1
    • 3543072944 scopus 로고    scopus 로고
    • Active Rho is localized to podosomes induced by oncogenic Src and is required for their assembly and function
    • R.L. Berdeaux B. Diaz L. Kim and G.S. Martin Active Rho is localized to podosomes induced by oncogenic Src and is required for their assembly and function J. Cell Biol. 166 2004 317-323
    • (2004) J. Cell Biol. , vol.166 , pp. 317-323
    • Berdeaux, R.L.1    Diaz, B.2    Kim, L.3    Martin, G.S.4
  • 2
    • 0031025999 scopus 로고    scopus 로고
    • The PDGF receptor phosphorylates Tyr 138 in the c-Src SH3 domain in vivo reducing peptide ligand binding
    • M.A. Broome and T. Hunter The PDGF receptor phosphorylates Tyr 138 in the c-Src SH3 domain in vivo reducing peptide ligand binding Oncogene 14 1997 17-34
    • (1997) Oncogene , vol.14 , pp. 17-34
    • Broome, M.A.1    Hunter, T.2
  • 3
    • 13944282937 scopus 로고    scopus 로고
    • Identification of Src-specific phosphorylation site on focal adhesion kinase: Dissection of the role of Src SH2 and catalytic functions and their consequences for tumor cell behavior
    • V.G. Brunton E. Avizienyte V.J. Fincham B. Serrels C.A. Metcalf 3rd T.K. Sawyer and M.C. Frame Identification of Src-specific phosphorylation site on focal adhesion kinase: Dissection of the role of Src SH2 and catalytic functions and their consequences for tumor cell behavior Cancer Res. 65 2005 1335-1342
    • (2005) Cancer Res. , vol.65 , pp. 1335-1342
    • Brunton, V.G.1    Avizienyte, E.2    Fincham, V.J.3    Serrels, B.4    Metcalf III, C.A.5    Sawyer, T.K.6    Frame, M.C.7
  • 4
    • 0034044795 scopus 로고    scopus 로고
    • Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: Correlation with preinvasive and invasive phenotypes
    • W.G. Cance J.E. Harris M.V. Iacocca E. Roche X. Yang J. Chang S. Simkins and L. Xu Immunohistochemical analyses of focal adhesion kinase expression in benign and malignant human breast and colon tissues: correlation with preinvasive and invasive phenotypes Clin. Cancer Res. 6 2000 2417-2423
    • (2000) Clin. Cancer Res. , vol.6 , pp. 2417-2423
    • Cance, W.G.1    Harris, J.E.2    Iacocca, M.V.3    Roche, E.4    Yang, X.5    Chang, J.6    Simkins, S.7    Xu, L.8
  • 5
    • 0032544735 scopus 로고    scopus 로고
    • Regulated endocytosis of G-protein-coupled receptors by a biochemically and functionally distinct subpopulation of clathrin-coated pits
    • T.T. Cao R.W. Mays and M. von Zastrow Regulated endocytosis of G-protein-coupled receptors by a biochemically and functionally distinct subpopulation of clathrin-coated pits J. Biol. Chem. 273 1998 24592-24602
    • (1998) J. Biol. Chem. , vol.273 , pp. 24592-24602
    • Cao, T.T.1    Mays, R.W.2    von Zastrow, M.3
  • 6
    • 0033527653 scopus 로고    scopus 로고
    • The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity
    • G. Cestra L. Castagnoli L. Dente O. Minenkova A. Petrelli N. Migone U. Hoffmuller J. Schneider-Mergener and G. Cesareni The SH3 domains of endophilin and amphiphysin bind to the proline-rich region of synaptojanin 1 at distinct sites that display an unconventional binding specificity J. Biol. Chem. 274 1999 32001-32007
    • (1999) J. Biol. Chem. , vol.274 , pp. 32001-32007
    • Cestra, G.1    Castagnoli, L.2    Dente, L.3    Minenkova, O.4    Petrelli, A.5    Migone, N.6    Hoffmuller, U.7    Schneider-Mergener, J.8    Cesareni, G.9
  • 7
    • 0036674501 scopus 로고    scopus 로고
    • Dissemination and growth of cancer cells in metastatic sites
    • A.F. Chambers A.C. Groom and I.C. MacDonald Dissemination and growth of cancer cells in metastatic sites Nat. Rev. Cancer 2 2002 563-572
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 563-572
    • Chambers, A.F.1    Groom, A.C.2    MacDonald, I.C.3
  • 8
    • 0022559078 scopus 로고
    • Tyr527 is phosphorylated in pp60c-src: Implications for regulation
    • J.A. Cooper K.L. Gould C.A. Cartwright and T. Hunter Tyr527 is phosphorylated in pp60c-src: Implications for regulation Science 231 1986 1431-1434
    • (1986) Science , vol.231 , pp. 1431-1434
    • Cooper, J.A.1    Gould, K.L.2    Cartwright, C.A.3    Hunter, T.4
  • 10
    • 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 Nat. Rev. Cancer 2 2002 161-174
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 11
    • 0035889088 scopus 로고    scopus 로고
    • Generation of high curvature membranes mediated by direct endophilin bilayer interactions
    • K. Farsad N. Ringstad K. Takei S.R. Floyd K. Rose and P. De Camilli Generation of high curvature membranes mediated by direct endophilin bilayer interactions J. Cell Biol. 155 2001 193-200
    • (2001) J. Cell Biol. , vol.155 , pp. 193-200
    • Farsad, K.1    Ringstad, N.2    Takei, K.3    Floyd, S.R.4    Rose, K.5    De Camilli, P.6
  • 12
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • D. Hanahan and R.A. Weinberg The hallmarks of cancer Cell 100 2000 57-70
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 13
    • 0037011055 scopus 로고    scopus 로고
    • FRNK blocks v-Src-stimulated invasion and experimental metastases without effects on cell motility or growth
    • C.R. Hauck D.A. Hsia X.S. Puente D.A. Cheresh and D.D. Schlaepfer FRNK blocks v-Src-stimulated invasion and experimental metastases without effects on cell motility or growth EMBO J. 21 2002 6289-6302
    • (2002) EMBO J. , vol.21 , pp. 6289-6302
    • Hauck, C.R.1    Hsia, D.A.2    Puente, X.S.3    Cheresh, D.A.4    Schlaepfer, D.D.5
  • 14
    • 0029955660 scopus 로고    scopus 로고
    • An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase
    • J.D. Hildebrand J.M. Taylor and J.T. Parsons An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase Mol. Cell. Biol. 16 1996 3169-3178
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3169-3178
    • Hildebrand, J.D.1    Taylor, J.M.2    Parsons, J.T.3
  • 15
    • 0036488589 scopus 로고    scopus 로고
    • Role of integrins in cell invasion and migration
    • J.D. Hood and D.A. Cheresh Role of integrins in cell invasion and migration Nat. Rev. Cancer 2 2002 91-100
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 91-100
    • Hood, J.D.1    Cheresh, D.A.2
  • 17
    • 0035923669 scopus 로고    scopus 로고
    • Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis
    • A. Jiang K. Lehti X. Wang S.J. Weiss J. Keski-Oja and D. Pei Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis Proc. Natl. Acad. Sci. USA 98 2001 13693-13698
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13693-13698
    • Jiang, A.1    Lehti, K.2    Wang, X.3    Weiss, S.J.4    Keski-Oja, J.5    Pei, D.6
  • 18
    • 0031657454 scopus 로고    scopus 로고
    • Focal adhesion kinase and its potential involvement in tumor invasion and metastasis
    • L.J. Kornberg Focal adhesion kinase and its potential involvement in tumor invasion and metastasis Head Neck 20 1998 745-752
    • (1998) Head Neck , vol.20 , pp. 745-752
    • Kornberg, L.J.1
  • 19
    • 0038433238 scopus 로고    scopus 로고
    • Podosomes: Adhesion hot-spots of invasive cells
    • S. Linder and M. Aepfelbacher Podosomes: Adhesion hot-spots of invasive cells Trends Cell Biol. 13 2003 376-385
    • (2003) Trends Cell Biol. , vol.13 , pp. 376-385
    • Linder, S.1    Aepfelbacher, M.2
  • 20
    • 0035985220 scopus 로고    scopus 로고
    • The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly
    • Y. Liu J.C. Loijens K.H. Martin A.V. Karginov and J.T. Parsons The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly Mol. Biol. Cell 13 2002 2147-2156
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2147-2156
    • Liu, Y.1    Loijens, J.C.2    Martin, K.H.3    Karginov, A.V.4    Parsons, J.T.5
  • 21
    • 0034176764 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Multifunctional contributors to tumor progression
    • L.J. McCawley and L.M. Matrisian Matrix metalloproteinases: multifunctional contributors to tumor progression Mol. Med. Today 6 2000 149-156
    • (2000) Mol. Med. Today , vol.6 , pp. 149-156
    • McCawley, L.J.1    Matrisian, L.M.2
  • 26
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • J.T. Parsons Focal adhesion kinase: The first ten years J. Cell Sci. 116 2003 1409-1416
    • (2003) J. Cell Sci. , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 27
    • 0142011033 scopus 로고    scopus 로고
    • Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface
    • A. Remacle G. Murphy and C. Roghi Membrane type I-matrix metalloproteinase (MT1-MMP) is internalised by two different pathways and is recycled to the cell surface J. Cell Sci. 116 2003 3905-3916
    • (2003) J. Cell Sci. , vol.116 , pp. 3905-3916
    • Remacle, A.1    Murphy, G.2    Roghi, C.3
  • 29
    • 0030739938 scopus 로고    scopus 로고
    • The SH3p4/Sh3p8/SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain
    • N. Ringstad Y. Nemoto and P. De Camilli The SH3p4/Sh3p8/SH3p13 protein family: Binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain Proc. Natl. Acad. Sci. USA 94 1997 8569-8574
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 8569-8574
    • Ringstad, N.1    Nemoto, Y.2    De Camilli, P.3
  • 30
    • 0034769929 scopus 로고    scopus 로고
    • Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src
    • P.J. Ruest N.Y. Shin T.R. Polte X. Zhang and S.K. Hanks Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src Mol. Cell. Biol. 21 2001 7641-7652
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7641-7652
    • Ruest, P.J.1    Shin, N.Y.2    Polte, T.R.3    Zhang, X.4    Hanks, S.K.5
  • 33
    • 0842281489 scopus 로고    scopus 로고
    • Multiple connections link FAK to cell motility and invasion
    • D.D. Schlaepfer and S.K. Mitra Multiple connections link FAK to cell motility and invasion Curr. Opin. Genet. Dev. 14 2004 92-101
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 92-101
    • Schlaepfer, D.D.1    Mitra, S.K.2
  • 35
    • 0037426578 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase: A key enzyme for tumor invasion
    • M. Seiki Membrane-type 1 matrix metalloproteinase: A key enzyme for tumor invasion Cancer Lett. 194 2003 1-11
    • (2003) Cancer Lett. , vol.194 , pp. 1-11
    • Seiki, M.1
  • 36
    • 0022357441 scopus 로고
    • Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes
    • G. Tarone D. Cirillo F.G. Giancotti P.M. Comoglio and P.C. Marchisio Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes Exp. Cell Res. 159 1985 141-157
    • (1985) Exp. Cell Res. , vol.159 , pp. 141-157
    • Tarone, G.1    Cirillo, D.2    Giancotti, F.G.3    Comoglio, P.M.4    Marchisio, P.C.5
  • 37
    • 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 J. Cell Biol. 155 2001 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
  • 38
    • 0034866603 scopus 로고    scopus 로고
    • Multiple pathways for the dynamin-regulated internalization of muscarinic acetylcholine receptors
    • C.J. van Koppen Multiple pathways for the dynamin-regulated internalization of muscarinic acetylcholine receptors Biochem. Soc. Trans. 29 2001 505-508
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 505-508
    • van Koppen, C.J.1
  • 39
    • 0032146236 scopus 로고    scopus 로고
    • The amphiphysin family of proteins and their role in endocytosis at the synapse
    • P. Wigge and H.T. McMahon The amphiphysin family of proteins and their role in endocytosis at the synapse Trends Neurosci. 21 1998 339-344
    • (1998) Trends Neurosci. , vol.21 , pp. 339-344
    • Wigge, P.1    McMahon, H.T.2
  • 40
    • 0031564611 scopus 로고    scopus 로고
    • Solution structure of the Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS: Direct refinement against NOEs, J-couplings and 1H and 13C chemical shifts
    • M. Wittekind C. Mapelli V. Lee V. Goldfarb M.S. Friedrichs C.A. Meyers and L. Mueller Solution structure of the Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS: Direct refinement against NOEs, J-couplings and 1H and 13C chemical shifts J. Mol. Biol. 267 1997 933-952
    • (1997) J. Mol. Biol. , vol.267 , pp. 933-952
    • Wittekind, M.1    Mapelli, C.2    Lee, V.3    Goldfarb, V.4    Friedrichs, M.S.5    Meyers, C.A.6    Mueller, L.7
  • 41
    • 1542304700 scopus 로고    scopus 로고
    • Focal adhesion kinase regulation of N-WASP subcellular localization and function
    • X. Wu S. Suetsugu L.A. Cooper T. Takenawa and J.L. Guan Focal adhesion kinase regulation of N-WASP subcellular localization and function J. Biol. Chem. 279 2004 9565-9576
    • (2004) J. Biol. Chem. , vol.279 , pp. 9565-9576
    • Wu, X.1    Suetsugu, S.2    Cooper, L.A.3    Takenawa, T.4    Guan, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.