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Volumn 18, Issue 14, 1999, Pages 3909-3923

PKCα regulates β1 integrin-dependent cell motility through association and control of integrin traffic

Author keywords

Endocytosis; FRET; GFP; Integrin; Migration; Protein kinase C

Indexed keywords

DYNAMIN; INTEGRIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE C; BETA1 INTEGRIN; CALCIUM; HYBRID PROTEIN; PHORBOL 13 ACETATE 12 MYRISTATE; SCLEROPROTEIN; TRANSFERRIN RECEPTOR;

EID: 0033565261     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/18.14.3909     Document Type: Article
Times cited : (285)

References (78)
  • 1
    • 0032937051 scopus 로고    scopus 로고
    • Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis
    • Achiriloaie, M., Barylko, B. and Albanesi, J.P. (1999) Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis. Mol. Cell. Biol., 19, 1410-1415.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1410-1415
    • Achiriloaie, M.1    Barylko, B.2    Albanesi, J.P.3
  • 2
    • 0031051255 scopus 로고    scopus 로고
    • Ectopic expression of a mutant form of PKCα originally found in human tumors: Aberrant subcellular translocation and effects on growth control
    • Alvaro, V., Prevostel, C., Joubert, D., Slosberg, E. and Weinstein, B.I. (1997) Ectopic expression of a mutant form of PKCα originally found in human tumors: aberrant subcellular translocation and effects on growth control. Oncogene, 14, 677-685.
    • (1997) Oncogene , vol.14 , pp. 677-685
    • Alvaro, V.1    Prevostel, C.2    Joubert, D.3    Slosberg, E.4    Weinstein, B.I.5
  • 4
    • 0001385205 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer microscopy
    • Celis, J.E. (ed.), Academic Press, New York, NY
    • Bastiaens, P.I.H. and Jovin, T.M. (1998) Fluorescence resonance energy transfer microscopy. In Celis, J.E. (ed.), Cell Biology: A Laboratory Handbook. Academic Press, New York, NY, pp. 136-146.
    • (1998) Cell Biology: A Laboratory Handbook , pp. 136-146
    • Bastiaens, P.I.H.1    Jovin, T.M.2
  • 5
    • 0033082668 scopus 로고    scopus 로고
    • Fluorescence lifetime imaging microscopy: Spatial resolution of biochemical processes in the cell
    • Bastiaens, P.I.H. and Squire, A. (1999) Fluorescence lifetime imaging microscopy: spatial resolution of biochemical processes in the cell. Trends Cell Biol., 9, 48-52.
    • (1999) Trends Cell Biol. , vol.9 , pp. 48-52
    • Bastiaens, P.I.H.1    Squire, A.2
  • 6
    • 0031952651 scopus 로고    scopus 로고
    • Are changes in integrin affinity and conformation overemphasized?
    • Bazzoni, G. and Hemler, M.E. (1998) Are changes in integrin affinity and conformation overemphasized? Trends Biochem. Sci., 23, 30-34.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 30-34
    • Bazzoni, G.1    Hemler, M.E.2
  • 7
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau, N., Sympson, C.J., Werb, Z. and Bissell, M.J. (1995) Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science, 267, 891-893.
    • (1995) Science , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.J.4
  • 8
    • 0032487438 scopus 로고    scopus 로고
    • Fibronectin matrix regulates activation of Rho and cdc42 GTPases and cell cycle progression
    • Bourdoulous, S., Orend, G., MacKenna, D.A., Pasqualini, R. and Ruoslahti, E. (1998) Fibronectin matrix regulates activation of Rho and cdc42 GTPases and cell cycle progression. J. Cell Biol., 143, 267-276.
    • (1998) J. Cell Biol. , vol.143 , pp. 267-276
    • Bourdoulous, S.1    Orend, G.2    MacKenna, D.A.3    Pasqualini, R.4    Ruoslahti, E.5
  • 9
    • 0032544735 scopus 로고    scopus 로고
    • Regulated endocytosis of G-protein-coupled receptors by a biochemically and functionally distinct subpopulation of clathrin-coated pits
    • Cao, T.T., Mays, R.W. and von Zastrow, M. (1998) Regulated endocytosis of G-protein-coupled receptors by a biochemically and functionally distinct subpopulation of clathrin-coated pits. J. Biol. Chem., 273, 24592-24602.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24592-24602
    • Cao, T.T.1    Mays, R.W.2    Von Zastrow, M.3
  • 10
    • 0032951298 scopus 로고    scopus 로고
    • Association of Rab25 abd Rab11a with the apical recycling system of polarized Madin-Darby Canine kidney cells
    • Casanova, J.E., Wang, X. and Kumar, R. (1999) Association of Rab25 abd Rab11a with the apical recycling system of polarized Madin-Darby Canine kidney cells. Mol. Biol. Cell, 10, 47-61.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 47-61
    • Casanova, J.E.1    Wang, X.2    Kumar, R.3
  • 11
    • 0030728127 scopus 로고    scopus 로고
    • Arachidonate initiated protein kinase C activation regulates HeLa cell spreading on a gelatin substrate by inducing F-actin formation and exocytotic upregulation of β1 integrin
    • Chun, J., Auer, K.A. and Jacobson, B.S. (1997) Arachidonate initiated protein kinase C activation regulates HeLa cell spreading on a gelatin substrate by inducing F-actin formation and exocytotic upregulation of β1 integrin. J. Cell Physiol., 173, 361-370.
    • (1997) J. Cell Physiol. , vol.173 , pp. 361-370
    • Chun, J.1    Auer, K.A.2    Jacobson, B.S.3
  • 12
    • 0030944210 scopus 로고    scopus 로고
    • Calmodulin regulates endosome fusion
    • Colombo, M.I., Beron, W. and Stahl, P.D. (1997) Calmodulin regulates endosome fusion. J. Biol. Chem., 272, 7707-7712.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7707-7712
    • Colombo, M.I.1    Beron, W.2    Stahl, P.D.3
  • 13
    • 0032173443 scopus 로고    scopus 로고
    • B1 integrin cytoplasmic domain regulates the constitutive conformation detected by MAb 15/7, but not the ligand-induced conformation
    • Crommie, D. and Hemler, M.E. (1998) B1 integrin cytoplasmic domain regulates the constitutive conformation detected by MAb 15/7, but not the ligand-induced conformation. J. Cell. Biochem., 71, 63-73.
    • (1998) J. Cell. Biochem. , vol.71 , pp. 63-73
    • Crommie, D.1    Hemler, M.E.2
  • 14
    • 0029890020 scopus 로고    scopus 로고
    • Targeted proteolysis of the focal adhesion kinase pp125FAK during c-Myc-induced apoptosis is suppressed by integrin signalling
    • Crouch, D.H., Fincham, V.J. and Frame, M.C. (1996) Targeted proteolysis of the focal adhesion kinase pp125FAK during c-Myc-induced apoptosis is suppressed by integrin signalling. Oncogene, 12, 2689-2696.
    • (1996) Oncogene , vol.12 , pp. 2689-2696
    • Crouch, D.H.1    Fincham, V.J.2    Frame, M.C.3
  • 15
    • 0031975838 scopus 로고    scopus 로고
    • Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase
    • Daaka, Y., Luttrell, L.M., Ahn, S., Rocca, G.J.D., Ferguson, S.S.G., Caron, M.G. and Lefkowitz, R.J. (1998) Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase. J. Biol. Chem., 273, 685-688.
    • (1998) J. Biol. Chem. , vol.273 , pp. 685-688
    • Daaka, Y.1    Luttrell, L.M.2    Ahn, S.3    Rocca, G.J.D.4    Ferguson, S.S.G.5    Caron, M.G.6    Lefkowitz, R.J.7
  • 16
    • 0026574126 scopus 로고
    • Kinetics of binding, endocytosis and recycling of EGF receptor mutants
    • Felder, S., LaVin, J., Ullrich, A. and Schlessinger, J. (1992) Kinetics of binding, endocytosis and recycling of EGF receptor mutants. J. Cell Biol., 117, 203-212.
    • (1992) J. Cell Biol. , vol.117 , pp. 203-212
    • Felder, S.1    LaVin, J.2    Ullrich, A.3    Schlessinger, J.4
  • 17
    • 0028111534 scopus 로고
    • A β turn in the cytoplasmic tail of the integrin αv subunit influences conformation and ligand binding of αvβ3
    • Filardo, E.J. and Cheresh, D.A. (1994) A β turn in the cytoplasmic tail of the integrin αv subunit influences conformation and ligand binding of αvβ3. J. Biol. Chem., 269, 4641-4647.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4641-4647
    • Filardo, E.J.1    Cheresh, D.A.2
  • 18
    • 0029050683 scopus 로고
    • Requirement of the NPXY motif in the integrin β 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo
    • Filardo, E.J., Brooks, P.C., Deming, S.L., Damsky, C. and Cheresh, D.A. (1995) Requirement of the NPXY motif in the integrin β 3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo. J. Cell Biol., 130, 441-450.
    • (1995) J. Cell Biol. , vol.130 , pp. 441-450
    • Filardo, E.J.1    Brooks, P.C.2    Deming, S.L.3    Damsky, C.4    Cheresh, D.A.5
  • 19
    • 0025362679 scopus 로고
    • Inhibition of binding of fibronectin to matrix assembly sites by anti-integrin (α 5 β 1) antibodies
    • Fogerty, F.J., Akiyama, S.K., Yamada, K.M. and Mosher, D.F. (1990) Inhibition of binding of fibronectin to matrix assembly sites by anti-integrin (α 5 β 1) antibodies. J. Cell Biol., 111, 699-708.
    • (1990) J. Cell Biol. , vol.111 , pp. 699-708
    • Fogerty, F.J.1    Akiyama, S.K.2    Yamada, K.M.3    Mosher, D.F.4
  • 20
    • 0030458602 scopus 로고    scopus 로고
    • A role for Jun-N-terminal kinase in anoikis; suppression by bc1-2 and crmA
    • Frisch, S.M., Vuori, K., Kelaita, D. and Sicks, S. (1996a) A role for Jun-N-terminal kinase in anoikis; suppression by bc1-2 and crmA. J. Cell Biol., 135, 1377-1382.
    • (1996) J. Cell Biol. , vol.135 , pp. 1377-1382
    • Frisch, S.M.1    Vuori, K.2    Kelaita, D.3    Sicks, S.4
  • 21
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch, S.M., Vuori, K., Ruoslahti, E. and Chan-Hui, P.Y. (1996b) Control of adhesion-dependent cell survival by focal adhesion kinase. J. Cell Biol., 134, 793-799.
    • (1996) J. Cell Biol. , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.Y.4
  • 22
    • 0029979181 scopus 로고    scopus 로고
    • Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature and then fuse directly with lysosomes
    • Futter, C.E., Pearse, A., Hewlett, L.J. and Hopkins, C.R. (1996) Multivesicular endosomes containing internalized EGF-EGF receptor complexes mature and then fuse directly with lysosomes. J. Cell Biol., 132, 1011-1023.
    • (1996) J. Cell Biol. , vol.132 , pp. 1011-1023
    • Futter, C.E.1    Pearse, A.2    Hewlett, L.J.3    Hopkins, C.R.4
  • 23
    • 0032143922 scopus 로고    scopus 로고
    • The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation
    • Garcia-Paramio, P., Cabrerizo, Y., Bornancin, F. and Parker, P.J. (1998) The broad specificity of dominant inhibitory protein kinase C mutants infers a common step in phosphorylation. Biochem. J., 333, 631-636.
    • (1998) Biochem. J. , vol.333 , pp. 631-636
    • Garcia-Paramio, P.1    Cabrerizo, Y.2    Bornancin, F.3    Parker, P.J.4
  • 24
    • 0026628625 scopus 로고
    • Synergistic activation of phospholipase D by protein kinase C- and G-protein-mediated pathways in streptolysin O-permeabilized HL60 cells
    • Geny, B. and Cockcroft, S. (1992) Synergistic activation of phospholipase D by protein kinase C-and G-protein-mediated pathways in streptolysin O-permeabilized HL60 cells. Biochem. J., 284, 531-538.
    • (1992) Biochem. J. , vol.284 , pp. 531-538
    • Geny, B.1    Cockcroft, S.2
  • 25
    • 0032563568 scopus 로고    scopus 로고
    • An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells
    • Ghosh, R.N., Mallet, W.G., Soe, T.T., McGraw, T.E. and Maxfield, F.R. (1998) An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells. J. Cell Biol., 142, 923-936.
    • (1998) J. Cell Biol. , vol.142 , pp. 923-936
    • Ghosh, R.N.1    Mallet, W.G.2    Soe, T.T.3    McGraw, T.E.4    Maxfield, F.R.5
  • 26
    • 0029059548 scopus 로고
    • Distinct functions for the two importin subunits in nuclear protein import
    • Gorlich, D., Vogel, F., Mills, A.D., Hartmann, E. and Laskey, R.A. (1995) Distinct functions for the two importin subunits in nuclear protein import. Nature, 377, 246-248.
    • (1995) Nature , vol.377 , pp. 246-248
    • Gorlich, D.1    Vogel, F.2    Mills, A.D.3    Hartmann, E.4    Laskey, R.A.5
  • 27
    • 0029100974 scopus 로고
    • Membrane transport in the endocytic pathway
    • Gruenberg, J. and Maxfield, F.R. (1995) Membrane transport in the endocytic pathway. Curr. Opin. Cell Biol., 7, 552-563.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 552-563
    • Gruenberg, J.1    Maxfield, F.R.2
  • 28
    • 0025223081 scopus 로고
    • Turning off the signal: Desensitization of β-adrenergic receptor function
    • Hausdorff, W.P., Caron, M.G. and Lefkowitz, R.J. (1990) Turning off the signal: desensitization of β-adrenergic receptor function. FASEB J., 4, 2881-2889.
    • (1990) FASEB J. , vol.4 , pp. 2881-2889
    • Hausdorff, W.P.1    Caron, M.G.2    Lefkowitz, R.J.3
  • 29
    • 0030636791 scopus 로고    scopus 로고
    • Triggering of motile behavior in T lymphocytes via cross-linking of α4 β1 and αL β2
    • Hauzenberger, D., Klominek, J., Holgersson, J., Bergstrom, S.E. and Sundqvist, K.G. (1997) Triggering of motile behavior in T lymphocytes via cross-linking of α4 β1 and αL β2. J. Immunol., 158, 76-84.
    • (1997) J. Immunol. , vol.158 , pp. 76-84
    • Hauzenberger, D.1    Klominek, J.2    Holgersson, J.3    Bergstrom, S.E.4    Sundqvist, K.G.5
  • 30
    • 0030272101 scopus 로고    scopus 로고
    • Integrin activation: The link between ligand binding and signal transduction
    • Humphries, M.J. (1996) Integrin activation: the link between ligand binding and signal transduction. Curr. Opin. Cell Biol., 8, 632-640.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 632-640
    • Humphries, M.J.1
  • 31
    • 0027368165 scopus 로고
    • Structure and mechanism of the G protein-coupled receptor kinases
    • Inglese, J., Freedman, N.J., Koch, W.J. and Lefkowitz, R.J. (1993) Structure and mechanism of the G protein-coupled receptor kinases. J. Biol. Chem., 268, 23735-23738.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23735-23738
    • Inglese, J.1    Freedman, N.J.2    Koch, W.J.3    Lefkowitz, R.J.4
  • 32
    • 0024363589 scopus 로고
    • Immunoaffinity purification of tyrosine-phosphorylated cellular proteins
    • Kanner, S.B., Reynolds, A.B. and Parsons, J.T. (1989) Immunoaffinity purification of tyrosine-phosphorylated cellular proteins. J. Immunol. Methods, 120, 115-124.
    • (1989) J. Immunol. Methods , vol.120 , pp. 115-124
    • Kanner, S.B.1    Reynolds, A.B.2    Parsons, J.T.3
  • 33
    • 0031032370 scopus 로고    scopus 로고
    • Defective microtubule reorganisation in phorbol ester-resistant U937 variants - Reconstitution of the normal-cell phenotype with nocodazole
    • Kiley, S.C. and Parker, P.J. (1997) Defective microtubule reorganisation in phorbol ester-resistant U937 variants - reconstitution of the normal-cell phenotype with nocodazole. Cell Growth Differ., 8, 231-242.
    • (1997) Cell Growth Differ. , vol.8 , pp. 231-242
    • Kiley, S.C.1    Parker, P.J.2
  • 34
    • 0031014916 scopus 로고    scopus 로고
    • Cloning and characterisation of phorbol ester differentiation-resistant U937 cell variants
    • Kiley, S.C., Adams, P.D. and Parker, P.J. (1997) Cloning and characterisation of phorbol ester differentiation-resistant U937 cell variants. Cell Growth Differ., 8, 221-230.
    • (1997) Cell Growth Differ. , vol.8 , pp. 221-230
    • Kiley, S.C.1    Adams, P.D.2    Parker, P.J.3
  • 35
    • 0028043735 scopus 로고
    • Receptor tyrosine kinase signaling required for integrin αVβ5-directed cell motility but not adhesion on vitronectin
    • Klemke, R.L., Yebra, M., Bayna, E.M. and Cheresh, D.A. (1994) Receptor tyrosine kinase signaling required for integrin αVβ5-directed cell motility but not adhesion on vitronectin. J. Cell Biol., 127, 859-866.
    • (1994) J. Cell Biol. , vol.127 , pp. 859-866
    • Klemke, R.L.1    Yebra, M.2    Bayna, E.M.3    Cheresh, D.A.4
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D.A. and Horwitz, A.F. (1996) Cell migration: a physically integrated molecular process. Cell, 84, 359-369.
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 38
    • 0028978448 scopus 로고
    • 2+ - And calcineurin-dependent recycling of an integrin to the front of the migrating neutrophils
    • 2+ - and calcineurin-dependent recycling of an integrin to the front of the migrating neutrophils. Nature, 377, 75-79.
    • (1995) Nature , vol.377 , pp. 75-79
    • Lawson, M.A.1    Maxfield, F.R.2
  • 39
    • 0027194487 scopus 로고
    • G protein-coupled receptor kinases
    • Lefkowitz, R.J. (1993) G protein-coupled receptor kinases. Cell, 74, 409-412.
    • (1993) Cell , vol.74 , pp. 409-412
    • Lefkowitz, R.J.1
  • 40
    • 0033610892 scopus 로고    scopus 로고
    • β-arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor 1 receptor
    • Lin, F.T., Daaka, Y. and Lefkowitz, R.J. (1998) β-arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor 1 receptor. J. Biol. Chem., 273, 31640-31643.
    • (1998) J. Biol. Chem. , vol.273 , pp. 31640-31643
    • Lin, F.T.1    Daaka, Y.2    Lefkowitz, R.J.3
  • 41
    • 0029956383 scopus 로고    scopus 로고
    • Integrin-dependent activation of the p70 ribosomal S6 kinase signaling pathway
    • Malik, R.K. and Parsons, J.T. (1996) Integrin-dependent activation of the p70 ribosomal S6 kinase signaling pathway. J. Biol. Chem., 271, 29785-29791.
    • (1996) J. Biol. Chem. , vol.271 , pp. 29785-29791
    • Malik, R.K.1    Parsons, J.T.2
  • 42
    • 0033056765 scopus 로고    scopus 로고
    • Amino acid motifs required for isolated β cytoplasmic domains to regulate 'in trans' β1 integrin conformation and function in cell attachment
    • Mastrangelo, A.M., Homan, S.M., Humphries, M.J. and LaFlamme, S.E. (1999) Amino acid motifs required for isolated β cytoplasmic domains to regulate 'in trans' β1 integrin conformation and function in cell attachment. J. Cell Sci., 112, 217-229.
    • (1999) J. Cell Sci. , vol.112 , pp. 217-229
    • Mastrangelo, A.M.1    Homan, S.M.2    Humphries, M.J.3    LaFlamme, S.E.4
  • 43
    • 0027243406 scopus 로고
    • Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process
    • Mayor, S., Presley, J.F. and Maxfield, F.R. (1993) Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process. J. Cell Biol., 121, 1257-1269.
    • (1993) J. Cell Biol. , vol.121 , pp. 1257-1269
    • Mayor, S.1    Presley, J.F.2    Maxfield, F.R.3
  • 44
    • 0032479979 scopus 로고    scopus 로고
    • A β1 integrin signaling pathway involving Src-family kinases, Cb1 and PI-3 kinase is required for macrophage spreading and migration
    • Meng, F. and Lowell, C.A. (1998) A β1 integrin signaling pathway involving Src-family kinases, Cb1 and PI-3 kinase is required for macrophage spreading and migration. EMBO J., 17, 4391-4403.
    • (1998) EMBO J. , vol.17 , pp. 4391-4403
    • Meng, F.1    Lowell, C.A.2
  • 45
    • 0027451706 scopus 로고
    • The extracellular matrix as a cell survival factor
    • Meredith, J.E., Fazeli, B. and Schwartz, M.A. (1993) The extracellular matrix as a cell survival factor. Mol. Biol. Cell, 4, 953-961.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 953-961
    • Meredith, J.E.1    Fazeli, B.2    Schwartz, M.A.3
  • 46
    • 0031594140 scopus 로고    scopus 로고
    • Expression of αv integrins and vitronectin receptor identity in breast cancer cells
    • Meyer, T., Marshall, J.F. and Hart, I.R. (1998) Expression of αv integrins and vitronectin receptor identity in breast cancer cells. Br. J. Cancer, 77, 530-536.
    • (1998) Br. J. Cancer , vol.77 , pp. 530-536
    • Meyer, T.1    Marshall, J.F.2    Hart, I.R.3
  • 47
    • 0032481142 scopus 로고    scopus 로고
    • Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav1
    • Miranti, C.K., Leng, L., Maschberger, P., Brugge, J.S. and Shattil, S.J. (1998) Identification of a novel integrin signaling pathway involving the kinase Syk and the guanine nucleotide exchange factor Vav1. Curr. Biol., 8, 1289-1299.
    • (1998) Curr. Biol. , vol.8 , pp. 1289-1299
    • Miranti, C.K.1    Leng, L.2    Maschberger, P.3    Brugge, J.S.4    Shattil, S.J.5
  • 48
    • 0028944308 scopus 로고
    • Identification of a novel anti-integrin monoclonal antibody that recognises a ligand-induced binding site epitope on the β1 subunit
    • Mould, A.P., Garratt, A.N., Askari, J.A., Akiyama, S.K. and Humphries, M.J. (1995) Identification of a novel anti-integrin monoclonal antibody that recognises a ligand-induced binding site epitope on the β1 subunit. FEBS Lett., 363, 118-122.
    • (1995) FEBS Lett. , vol.363 , pp. 118-122
    • Mould, A.P.1    Garratt, A.N.2    Askari, J.A.3    Akiyama, S.K.4    Humphries, M.J.5
  • 49
    • 0029664954 scopus 로고    scopus 로고
    • The inhibitory anti-β1 integrin monoclonal antibody 13 recognizes an epitope that is attenuated by ligand occupancy. Evidence for allosteric inhibition of integrin function
    • Mould, A.P., Akiyama, S.K. and Humphries, M.J. (1996) The inhibitory anti-β1 integrin monoclonal antibody 13 recognizes an epitope that is attenuated by ligand occupancy. Evidence for allosteric inhibition of integrin function. J. Biol. Chem., 271, 20365-20374.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20365-20374
    • Mould, A.P.1    Akiyama, S.K.2    Humphries, M.J.3
  • 50
    • 0032079781 scopus 로고    scopus 로고
    • Regulation of integrin function: Evidence that bivalent-cation-induced conformational changes lead to the unmasking of ligand-binding sites within integrin α5 β1
    • Mould, A.P., Garratt, A.N., Puzon-McLaughlin, W., Takada, Y. and Humphries, M.J. (1998) Regulation of integrin function: evidence that bivalent-cation-induced conformational changes lead to the unmasking of ligand-binding sites within integrin α5 β1. Biochem. J., 331, 821-828.
    • (1998) Biochem. J. , vol.331 , pp. 821-828
    • Mould, A.P.1    Garratt, A.N.2    Puzon-McLaughlin, W.3    Takada, Y.4    Humphries, M.J.5
  • 51
    • 0028950908 scopus 로고
    • Adhesion co-receptor expression and intracellular signalling in HIV disease: Implications for immunotherapy
    • Ng, T.T.C., Guntermann, C., Nye, K.E., Parkin, J.M., Anderson, J., Norman, J.E. and Morrow, W.J.W. (1995) Adhesion co-receptor expression and intracellular signalling in HIV disease: implications for immunotherapy. AIDS, 9, 337-343.
    • (1995) AIDS , vol.9 , pp. 337-343
    • Ng, T.T.C.1    Guntermann, C.2    Nye, K.E.3    Parkin, J.M.4    Anderson, J.5    Norman, J.E.6    Morrow, W.J.W.7
  • 53
    • 0033605542 scopus 로고    scopus 로고
    • Imaging protein kinase C α activation in cells
    • Ng, T. et al. (1999) Imaging protein kinase C α activation in cells. Science, 283, 2085-2089.
    • (1999) Science , vol.283 , pp. 2085-2089
    • Ng, T.1
  • 54
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium
    • Oh, P., McIntosh, D.P. and Schnitzer, J.E. (1998) Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fission from the plasma membrane of endothelium. J. Cell Biol., 141, 101-114.
    • (1998) J. Cell Biol. , vol.141 , pp. 101-114
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 55
    • 0025869231 scopus 로고
    • Down-regulation of a kinase defective PKC-a
    • Pears, C. and Parker, P.J. (1991) Down-regulation of a kinase defective PKC-a. FEBS Lett., 284, 120-122.
    • (1991) FEBS Lett. , vol.284 , pp. 120-122
    • Pears, C.1    Parker, P.J.2
  • 56
    • 0031283128 scopus 로고    scopus 로고
    • The integrin α6β4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures
    • Rabinovitz, I. and Mercurio, A.M. (1997) The integrin α6β4 functions in carcinoma cell migration on laminin-1 by mediating the formation and stabilization of actin-containing motility structures. J. Cell Biol., 139, 1873-1884.
    • (1997) J. Cell Biol. , vol.139 , pp. 1873-1884
    • Rabinovitz, I.1    Mercurio, A.M.2
  • 57
    • 0026642556 scopus 로고
    • Identification of amino acid sequences in the integrin β1 cytoplasmic domain implicated in cytoskeletal association
    • Reszka, A.A., Hayashi, Y. and Horwitz, A.F. (1992) Identification of amino acid sequences in the integrin β1 cytoplasmic domain implicated in cytoskeletal association. J. Cell Biol., 117, 1321-1330.
    • (1992) J. Cell Biol. , vol.117 , pp. 1321-1330
    • Reszka, A.A.1    Hayashi, Y.2    Horwitz, A.F.3
  • 59
    • 0031768408 scopus 로고    scopus 로고
    • Integrin ligation and PKC activation are required for migration of colon carcinoma cells
    • Rigot, V., Lehmann, M., Andre, F., Daemi, N., Marvaldi, J. and Luis, J. (1998) Integrin ligation and PKC activation are required for migration of colon carcinoma cells. J. Cell Sci., 111, 3119-3127.
    • (1998) J. Cell Sci. , vol.111 , pp. 3119-3127
    • Rigot, V.1    Lehmann, M.2    Andre, F.3    Daemi, N.4    Marvaldi, J.5    Luis, J.6
  • 60
    • 0032479156 scopus 로고    scopus 로고
    • High-affinity binding of epidermal growth factor (EGF) to EGF receptor is disrupted by overexpression of mutant dynamin (K44A)
    • Ringerike, T., Stang, E., Johannessen, L.E., Sandnes, D., Levy, F.O. and Madshus, I.H. (1998) High-affinity binding of epidermal growth factor (EGF) to EGF receptor is disrupted by overexpression of mutant dynamin (K44A). J. Biol. Chem., 273, 16639-16642.
    • (1998) J. Biol. Chem. , vol.273 , pp. 16639-16642
    • Ringerike, T.1    Stang, E.2    Johannessen, L.E.3    Sandnes, D.4    Levy, F.O.5    Madshus, I.H.6
  • 61
    • 0032584382 scopus 로고    scopus 로고
    • Restoration of β1A integrins is required for lysophosphatidic acid-induced migration of β 1-null mouse fibroblastic cells
    • Saka, T., Peyruchaud, O., Fassler, R. and Mosher, D.F. (1998) Restoration of β1A integrins is required for lysophosphatidic acid-induced migration of β 1-null mouse fibroblastic cells. J. Biol. Chem., 273, 19378-19382.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19378-19382
    • Saka, T.1    Peyruchaud, O.2    Fassler, R.3    Mosher, D.F.4
  • 62
    • 0032549860 scopus 로고    scopus 로고
    • Modulation of β1A integrin functions by tyrosine residues in the β1 cytoplasmic domain
    • Sakai, T., Zhang, Q., Fassler, R. and Mosher, D.F. (1998) Modulation of β1A integrin functions by tyrosine residues in the β1 cytoplasmic domain. J. Cell Biol., 141, 527-538.
    • (1998) J. Cell Biol. , vol.141 , pp. 527-538
    • Sakai, T.1    Zhang, Q.2    Fassler, R.3    Mosher, D.F.4
  • 63
    • 0242683360 scopus 로고    scopus 로고
    • Leukocyte polarization in cell migration and immune interactions
    • Sanchez-Madrid, F. and del Pozo, M.A. (1999) Leukocyte polarization in cell migration and immune interactions. EMBO J., 18, 501-511.
    • (1999) EMBO J. , vol.18 , pp. 501-511
    • Sanchez-Madrid, F.1    Del Pozo, M.A.2
  • 64
    • 0030814976 scopus 로고    scopus 로고
    • αVβ3 integrin associates with activated insulin and PDGF β receptors and potentiates the biological activity of PDGF
    • Schneller, M., Vuori, K. and Ruoslahti, E. (1997) αVβ3 integrin associates with activated insulin and PDGF β receptors and potentiates the biological activity of PDGF. EMBO J., 16, 5600-5607.
    • (1997) EMBO J. , vol.16 , pp. 5600-5607
    • Schneller, M.1    Vuori, K.2    Ruoslahti, E.3
  • 65
    • 0029812898 scopus 로고    scopus 로고
    • Protein kinase C deficiency blocks recovery from agonist-induced desensitization
    • Shih, M. and Malbon, C.C. (1996) Protein kinase C deficiency blocks recovery from agonist-induced desensitization. J. Biol. Chem., 271, 21478-21483.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21478-21483
    • Shih, M.1    Malbon, C.C.2
  • 66
    • 0032517624 scopus 로고    scopus 로고
    • Distinct roles for the p110α and hVPS34 phosphatidylinositol 3′-kinases in vesicular trafficking, regulation of the actin cytoskeleton and mitogenesis
    • Siddhanta, U., McIlroy, J., Shah, A., Zhang, Y. and Backer, J.M. (1998) Distinct roles for the p110α and hVPS34 phosphatidylinositol 3′-kinases in vesicular trafficking, regulation of the actin cytoskeleton and mitogenesis. J. Cell Biol., 143, 1647-1659.
    • (1998) J. Cell Biol. , vol.143 , pp. 1647-1659
    • Siddhanta, U.1    McIlroy, J.2    Shah, A.3    Zhang, Y.4    Backer, J.M.5
  • 67
    • 0029671455 scopus 로고    scopus 로고
    • Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity
    • Singer, W.D., Brown, H.A., Jiang, X. and Sternweis, P.C. (1996) Regulation of phospholipase D by protein kinase C is synergistic with ADP-ribosylation factor and independent of protein kinase activity. J. Biol. Chem., 271, 4504-4510.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4504-4510
    • Singer, W.D.1    Brown, H.A.2    Jiang, X.3    Sternweis, P.C.4
  • 68
    • 0032891840 scopus 로고    scopus 로고
    • Three dimensional image restoration in fluorescence lifetime imaging microscopy
    • Squire, A. and Bastiaens, P.I.H. (1999) Three dimensional image restoration in fluorescence lifetime imaging microscopy. J. Microsc., 193, 36-49.
    • (1999) J. Microsc. , vol.193 , pp. 36-49
    • Squire, A.1    Bastiaens, P.I.H.2
  • 69
    • 0029986708 scopus 로고    scopus 로고
    • Autocrine motility factor signals integrin-mediated metastatic melanoma cell adhesion and invasion
    • Timar, J., Trikha, M., Szekeres, K., Bazaz, R., Tovari, J., Silletti, S., Raz, A. and Honn, K.V. (1996) Autocrine motility factor signals integrin-mediated metastatic melanoma cell adhesion and invasion. Cancer Res., 56, 1902-1908.
    • (1996) Cancer Res. , vol.56 , pp. 1902-1908
    • Timar, J.1    Trikha, M.2    Szekeres, K.3    Bazaz, R.4    Tovari, J.5    Silletti, S.6    Raz, A.7    Honn, K.V.8
  • 70
    • 17544377292 scopus 로고    scopus 로고
    • ADP-ribosylation of the G protein Rho inhibits integrin regulation of tumor cell growth
    • Udagawa, T. and McIntyre, B.W. (1996) ADP-ribosylation of the G protein Rho inhibits integrin regulation of tumor cell growth. J. Biol. Chem., 271, 12542-12548.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12542-12548
    • Udagawa, T.1    McIntyre, B.W.2
  • 71
    • 0033545698 scopus 로고    scopus 로고
    • Importance of the pleckstrin homology domain of dynamin in clathrin-mediated endocytosis
    • Vallis, Y., Wigge, P., Marks, B., Evans, P.R. and McMahon, H.T. (1999) Importance of the pleckstrin homology domain of dynamin in clathrin-mediated endocytosis. Curr. Biol., 9, 257-260.
    • (1999) Curr. Biol. , vol.9 , pp. 257-260
    • Vallis, Y.1    Wigge, P.2    Marks, B.3    Evans, P.R.4    McMahon, H.T.5
  • 72
    • 0030584077 scopus 로고    scopus 로고
    • The adaptor protein Shc couples a class of integrins to the control of cell cycle progression
    • Wary, K.K., Mainiero, F., Isakoff, S.J., Marcantonio, E.E. and Giancotti, F.G. (1996) The adaptor protein Shc couples a class of integrins to the control of cell cycle progression. Cell, 87, 733-743.
    • (1996) Cell , vol.87 , pp. 733-743
    • Wary, K.K.1    Mainiero, F.2    Isakoff, S.J.3    Marcantonio, E.E.4    Giancotti, F.G.5
  • 73
    • 0032525350 scopus 로고    scopus 로고
    • β1 integrins are critically involved in neutrophil locomotion in extravascular tissue in vivo
    • Werr, J., Xie, X., Hedqvist, P., Ruoslahti, E. and Lindbom, L. (1998) β1 integrins are critically involved in neutrophil locomotion in extravascular tissue in vivo. J. Exp. Med., 187, 2091-2096.
    • (1998) J. Exp. Med. , vol.187 , pp. 2091-2096
    • Werr, J.1    Xie, X.2    Hedqvist, P.3    Ruoslahti, E.4    Lindbom, L.5
  • 74
    • 0030458832 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1-regulated phospholipase D activity is localized at the plasma membrane and intracellular organelles in HL60 cells
    • Whatmore, J., Morgan, C.P., Cunningham, E., Collison, K.S., Willison, K.R. and Cockcroft, S. (1996) ADP-ribosylation factor 1-regulated phospholipase D activity is localized at the plasma membrane and intracellular organelles in HL60 cells. Biochem. J., 320, 785-794.
    • (1996) Biochem. J. , vol.320 , pp. 785-794
    • Whatmore, J.1    Morgan, C.P.2    Cunningham, E.3    Collison, K.S.4    Willison, K.R.5    Cockcroft, S.6
  • 75
    • 0026603414 scopus 로고
    • Protein kinase C involvement in focal adhesion formation
    • Woods, A. and Couchman, J.R. (1992) Protein kinase C involvement in focal adhesion formation. J. Cell Sci., 101, 277-290.
    • (1992) J. Cell Sci. , vol.101 , pp. 277-290
    • Woods, A.1    Couchman, J.R.2
  • 76
    • 0029044627 scopus 로고
    • Induction of carcinoma cell migration on vitronectin by NF-kB-dependent gene expression
    • Yebra, M., Filardo, E.J., Bayna, E.M., Kawahara, E., Becker, J.C. and Cheresh, D.A. (1995) Induction of carcinoma cell migration on vitronectin by NF-kB-dependent gene expression. Mol. Biol. Cell, 6, 841-850.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 841-850
    • Yebra, M.1    Filardo, E.J.2    Bayna, E.M.3    Kawahara, E.4    Becker, J.C.5    Cheresh, D.A.6
  • 77
    • 0023900060 scopus 로고
    • A monoclonal antibody recognising the site of limited proteolysis of protein kinase C
    • Young, S., Rothbard, J. and Parker, P. (1988) A monoclonal antibody recognising the site of limited proteolysis of protein kinase C. Eur. J. Biochem., 173, 247-252.
    • (1988) Eur. J. Biochem. , vol.173 , pp. 247-252
    • Young, S.1    Rothbard, J.2    Parker, P.3
  • 78
    • 0029665783 scopus 로고    scopus 로고
    • Involvement of integrin αVβ3 in cell adhesion, motility and liver metastasis of murine RAW117 large cell lymphoma
    • Yun, Z., Menter, D.G. and Nicolson, G.L. (1996) Involvement of integrin αVβ3 in cell adhesion, motility and liver metastasis of murine RAW117 large cell lymphoma. Cancer Res., 56, 3103-3111.
    • (1996) Cancer Res. , vol.56 , pp. 3103-3111
    • Yun, Z.1    Menter, D.G.2    Nicolson, G.L.3


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