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Volumn 17, Issue 7, 1997, Pages 3841-3849

Phosphatidylinositol 4,5-bisphosphate phosphatase regulates the rearrangement of actin filaments

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; EPIDERMAL GROWTH FACTOR RECEPTOR; PHOSPHATASE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE;

EID: 0030981640     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.7.3841     Document Type: Article
Times cited : (149)

References (40)
  • 1
    • 0026742127 scopus 로고
    • The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase
    • Attree, O., I. M. Olivos, I. Okabe, L. C. Bailey, D. L. Nelson, R. A. Lewis, R. R. McInners, and R. L. Nussbaum. 1992. The Lowe's oculocerebrorenal syndrome gene encodes a protein highly homologous to inositol polyphosphate-5-phosphatase. Nature 358:239-242.
    • (1992) Nature , vol.358 , pp. 239-242
    • Attree, O.1    Olivos, I.M.2    Okabe, I.3    Bailey, L.C.4    Nelson, D.L.5    Lewis, R.A.6    McInners, R.R.7    Nussbaum, R.L.8
  • 2
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge, M. J. 1993. Inositol trisphosphate and calcium signalling. Nature 361:315-325.
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 3
    • 0027153103 scopus 로고
    • Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor
    • Buday, L., and J. Downward. 1993. Epidermal growth factor regulates p21ras through the formation of a complex of receptor, Grb2 adapter protein, and Sos nucleotide exchange factor. Cell 73:611-620.
    • (1993) Cell , vol.73 , pp. 611-620
    • Buday, L.1    Downward, J.2
  • 6
    • 0024828304 scopus 로고
    • Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function
    • Cleves, A. E., P. J. Novick, and V. A. Bankaitis. 1989. Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function. J. Cell Biol. 109:2939-2950.
    • (1989) J. Cell Biol. , vol.109 , pp. 2939-2950
    • Cleves, A.E.1    Novick, P.J.2    Bankaitis, V.A.3
  • 7
    • 0027910431 scopus 로고
    • Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
    • Egan, S. E., B. W. Giddings, M. W. Brooks, L. Buday, A. M. Siezland, and R. A. Weinberg. 1993. Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature 363:45-51.
    • (1993) Nature , vol.363 , pp. 45-51
    • Egan, S.E.1    Giddings, B.W.2    Brooks, M.W.3    Buday, L.4    Siezland, A.M.5    Weinberg, R.A.6
  • 8
    • 0027940655 scopus 로고
    • SH2 and SH3 domains as molecular adhesives: The interactions of Crk and Abl
    • Feller, S. M., R. Ren, H. Hanafusa, and D. Baltimore. 1994. SH2 and SH3 domains as molecular adhesives: the interactions of Crk and Abl. Trends Biochem. Sci. 19:453-458.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 453-458
    • Feller, S.M.1    Ren, R.2    Hanafusa, H.3    Baltimore, D.4
  • 9
    • 0026756594 scopus 로고
    • Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-actinin function
    • Fukami, K., K. Fumhashi, M. Inagaki, T. Endo, S. Hatano, and T. Takenawa. 1992. Requirement of phosphatidylinositol 4,5-bisphosphate for alpha-actinin function. Nature 359:150-152.
    • (1992) Nature , vol.359 , pp. 150-152
    • Fukami, K.1    Fumhashi, K.2    Inagaki, M.3    Endo, T.4    Hatano, S.5    Takenawa, T.6
  • 10
    • 0028174102 scopus 로고
    • Alpha-actinin and vinculin are PIP2-binding proteins involved in signaling by tyrosine kinase
    • Fukami, K., T. Endo, M. Inamura, and T. Takenawa. 1994. Alpha-actinin and vinculin are PIP2-binding proteins involved in signaling by tyrosine kinase. J. Biol. Chem. 269:1518-1522.
    • (1994) J. Biol. Chem. , vol.269 , pp. 1518-1522
    • Fukami, K.1    Endo, T.2    Inamura, M.3    Takenawa, T.4
  • 11
    • 0030043081 scopus 로고    scopus 로고
    • Identification of a phosphatidylinositol 4,5-bisphosphate-binding site in chicken skeletal muscle α-actinin
    • Fukami, K., N. Sawada, T. Endo, and T. Takenawa. 1996. Identification of a phosphatidylinositol 4,5-bisphosphate-binding site in chicken skeletal muscle α-actinin. J. Biol. Chem. 271:2646-2650.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2646-2650
    • Fukami, K.1    Sawada, N.2    Endo, T.3    Takenawa, T.4
  • 12
    • 0025760751 scopus 로고
    • Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation
    • Goldschmidt-Clermont, P. J., J. W. Kim, L. M. Machesky, S. G. Rhee, and T. D. Pollard. 1991. Regulation of phospholipase C-gamma 1 by profilin and tyrosine phosphorylation. Science 251:1231-1233.
    • (1991) Science , vol.251 , pp. 1231-1233
    • Goldschmidt-Clermont, P.J.1    Kim, J.W.2    Machesky, L.M.3    Rhee, S.G.4    Pollard, T.D.5
  • 14
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J. H., G. M. Bokoch, C. L. Carpenter, P. A. Janmey, L. A. Tayor, A. Toker, and T. P. Stossel. 1995. Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82:643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Tayor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 15
    • 0025880154 scopus 로고
    • Interaction of protein kinase C isozymes with phosphatidylinositol 4,5-bisphosphate
    • Huang, F. L., and K. P. Huang. 1991. Interaction of protein kinase C isozymes with phosphatidylinositol 4,5-bisphosphate. J. Biol. Chem. 266: 8727-8733.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8727-8733
    • Huang, F.L.1    Huang, K.P.2
  • 16
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate
    • Janmey, P. A., and T. P. Stossel. 1987. Modulation of gelsolin function by phosphatidylinositol 4,5-bisphosphate. Nature 325:362-364.
    • (1987) Nature , vol.325 , pp. 362-364
    • Janmey, P.A.1    Stossel, T.P.2
  • 17
    • 0025878284 scopus 로고
    • Polyproline affinity method for purification of platelet profilin and modification with pyrene-maleimide
    • Janmey, P. A. 1991. Polyproline affinity method for purification of platelet profilin and modification with pyrene-maleimide. Methods Enzymol. 196: 92-99.
    • (1991) Methods Enzymol. , vol.196 , pp. 92-99
    • Janmey, P.A.1
  • 18
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidylinositol 4,5-hisphosphate and profilactin
    • Lassing, I., and U. Lindberg. 1985. Specific interaction between phosphatidylinositol 4,5-hisphosphate and profilactin. Nature 314:472-474.
    • (1985) Nature , vol.314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 19
  • 20
    • 0029019442 scopus 로고
    • Signal transduction and membrane traffic: The PITP/phosphoinositide connection
    • Liscovitch, M., and L. C. Cantley. 1995. Signal transduction and membrane traffic: the PITP/phosphoinositide connection. Cell 81:659-662.
    • (1995) Cell , vol.81 , pp. 659-662
    • Liscovitch, M.1    Cantley, L.C.2
  • 22
    • 0029881416 scopus 로고    scopus 로고
    • Inositols do it all
    • Majerus, P. W. 1996. Inositols do it all. Genes Dev. 10:1051-1053.
    • (1996) Genes Dev. , vol.10 , pp. 1051-1053
    • Majerus, P.W.1
  • 23
    • 0026756438 scopus 로고
    • Cloning of ASH, a ubiquitous protein composed of one Src homology region (SH) 2 and two SH3 domains, from human and rat cDNA libraries
    • Matuoka, K., M. Shibata, A. Yamakawa, and T. Takenawa. 1992. Cloning of ASH, a ubiquitous protein composed of one Src homology region (SH) 2 and two SH3 domains, from human and rat cDNA libraries. Proc. Natl. Acad. Sci. USA 89:9015-9019.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9015-9019
    • Matuoka, K.1    Shibata, M.2    Yamakawa, A.3    Takenawa, T.4
  • 24
    • 0027217074 scopus 로고
    • Ash/Grb-2, a SH2/SH3-containing protein, couples to signaling for mitogenesis and cytoskeletal reorganization by EGF and PDGF
    • Matuoka, K., F. Shibasaki, M. Shibata, and T. Takenawa. 1993. Ash/Grb-2, a SH2/SH3-containing protein, couples to signaling for mitogenesis and cytoskeletal reorganization by EGF and PDGF. EMBO J. 12:3467-3473.
    • (1993) EMBO J. , vol.12 , pp. 3467-3473
    • Matuoka, K.1    Shibasaki, F.2    Shibata, M.3    Takenawa, T.4
  • 25
    • 0027965977 scopus 로고
    • Identification and characterization of the phosphatidylinositol 4,5-bisphosphate 5-phosphatase in human platelets
    • Matzaris, M., S. P. Jackson, K. M. Laxminarayan, C. J. Speed, and C. A. Mitchell. 1994. Identification and characterization of the phosphatidylinositol 4,5-bisphosphate 5-phosphatase in human platelets. J. Biol. Chem. 269: 3397-3402.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3397-3402
    • Matzaris, M.1    Jackson, S.P.2    Laxminarayan, K.M.3    Speed, C.J.4    Mitchell, C.A.5
  • 27
    • 0028885860 scopus 로고
    • Coupling of the proto-oncogene product c-Cbl to the epidermal growth factor receptor
    • Meisner, H., and M. P. Czech. 1995. Coupling of the proto-oncogene product c-Cbl to the epidermal growth factor receptor. J. Biol. Chem. 270:25332-25353.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25332-25353
    • Meisner, H.1    Czech, M.P.2
  • 29
    • 0029815611 scopus 로고    scopus 로고
    • N-WASP, a novel actin-de-polymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases
    • Miki, H., K. Miura, and T. Takenawa. 1996. N-WASP, a novel actin-de-polymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO J. 15:5325-5335.
    • (1996) EMBO J. , vol.15 , pp. 5325-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 30
    • 0029899089 scopus 로고    scopus 로고
    • Interaction of Ash/Grb2 via its SH3 domains with neuron-specific p150 and p65
    • Miura, K., H. Miki, K. Shimazaki, N. Kawai, and T. Takenawa. 1996. Interaction of Ash/Grb2 via its SH3 domains with neuron-specific p150 and p65. Biochem. J. 316:639-645.
    • (1996) Biochem. J. , vol.316 , pp. 639-645
    • Miura, K.1    Miki, H.2    Shimazaki, K.3    Kawai, N.4    Takenawa, T.5
  • 31
    • 0028955146 scopus 로고
    • Effects of cofilin on actin filamentous structures in cultured muscle cells. Intracellular regulation of cofilin action
    • Nagaoka, R., K. Kusano, H. Abe, and T. Obinata. 1995. Effects of cofilin on actin filamentous structures in cultured muscle cells. Intracellular regulation of cofilin action. J. Cell Sci. 108:581-593.
    • (1995) J. Cell Sci. , vol.108 , pp. 581-593
    • Nagaoka, R.1    Kusano, K.2    Abe, H.3    Obinata, T.4
  • 32
    • 0021227676 scopus 로고
    • The role of protein kinase C in cell surface signal transduction and tumor promotion
    • Nishizuka, Y. 1984. The role of protein kinase C in cell surface signal transduction and tumor promotion. Nature 308:693-698.
    • (1984) Nature , vol.308 , pp. 693-698
    • Nishizuka, Y.1
  • 33
    • 0028031152 scopus 로고
    • Purification of two immunologically related phosphatidylinositol 4,5-bisphosphate phosphatase from bovine brain cytosol
    • Palmer, K. B. S., R. Theolis, H. W. Cook, and D. Byers. 1994. Purification of two immunologically related phosphatidylinositol 4,5-bisphosphate phosphatase from bovine brain cytosol. J. Biol. Chem. 269:3403-3410.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3403-3410
    • Palmer, K.B.S.1    Theolis, R.2    Cook, H.W.3    Byers, D.4
  • 34
    • 0028278346 scopus 로고
    • GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids
    • Randazzo, P. A., and R. A. Kahn. 1994. GTP hydrolysis by ADP-ribosylation factor is dependent on both an ADP-ribosylation factor GTPase-activating protein and acid phospholipids. J. Biol. Chem. 269:10758-10763.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10758-10763
    • Randazzo, P.A.1    Kahn, R.A.2
  • 35
    • 0027294981 scopus 로고
    • The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
    • Rozakis-Adocock, M., R. Fernley, J. Wade, T. Pawson, and D. Bowtell. 1993. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Nature 363:83-85.
    • (1993) Nature , vol.363 , pp. 83-85
    • Rozakis-Adocock, M.1    Fernley, R.2    Wade, J.3    Pawson, T.4    Bowtell, D.5
  • 36
    • 0026454458 scopus 로고
    • Positive regulation of mu-calpain action by polyphosphoinositides
    • Saido, T. C., H. Suzuki, H. Yamazaki, K. Tanoue, and K. Suzuki. 1993. Positive regulation of mu-calpain action by polyphosphoinositides. J. Biol. Chem. 267:24585-24590.
    • (1993) J. Biol. Chem. , vol.267 , pp. 24585-24590
    • Saido, T.C.1    Suzuki, H.2    Yamazaki, H.3    Tanoue, K.4    Suzuki, K.5
  • 37
    • 0029097309 scopus 로고
    • Localization of a binding site for phosphatidylinositol 4,5-bisphosphate on human profilin
    • Sohn, R. H., J. Chen, K. S. Koblan, P. F. Bray, and P. J. Goldschmidt-Clermont. 1995. Localization of a binding site for phosphatidylinositol 4,5-bisphosphate on human profilin. J. Biol. Chem. 270:21114-21120.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21114-21120
    • Sohn, R.H.1    Chen, J.2    Koblan, K.S.3    Bray, P.F.4    Goldschmidt-Clermont, P.J.5
  • 38
    • 0026044059 scopus 로고
    • A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin
    • Yonezawa, N.,Y. Homma, I. Yahara, H. Sakai, and E. Nishida. 1991. A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin. J. Biol. Chem. 266:17218-17221.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17218-17221
    • Yonezawa, N.1    Homma, Y.2    Yahara, I.3    Sakai, H.4    Nishida, E.5
  • 39
    • 0025651999 scopus 로고
    • gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein
    • Yu, F. X., P. A. Johnston, T. C. Sudhof, and H. L. Yin. 1990. gCap39, a calcium ion-and polyphosphoinositide-regulated actin capping protein. Science 250:1413-1415.
    • (1990) Science , vol.250 , pp. 1413-1415
    • Yu, F.X.1    Johnston, P.A.2    Sudhof, T.C.3    Yin, H.L.4
  • 40
    • 0029060795 scopus 로고
    • The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphos-phate 5-phosphatase
    • Zhang, X., A. B. Jefferson, V. Auethavekiat, and P. W. Majerus. 1995. The protein deficient in Lowe syndrome is a phosphatidylinositol-4,5-bisphos-phate 5-phosphatase. Proc. Natl. Acad. Sci. USA 92:4853-4856.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4853-4856
    • Zhang, X.1    Jefferson, A.B.2    Auethavekiat, V.3    Majerus, P.W.4


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