메뉴 건너뛰기




Volumn 22, Issue 22, 2002, Pages 7953-7966

The cysteine-rich sprouty translocation domain targets mitogen-activated protein kinase inhibitory proteins to phosphatidylinositol 4,5-bisphosphate in plasma membranes

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CYSTEINE; IONOMYCIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; PHOSPHATASE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE C; PLECKSTRIN; PROTEIN; PROTEIN TYROSINE KINASE; RAS PROTEIN;

EID: 0036840415     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.22.22.7953-7966.2002     Document Type: Article
Times cited : (72)

References (33)
  • 1
    • 0033567293 scopus 로고    scopus 로고
    • DAPP1: A dual adaptor for phosphotyrosine and 3-phosphoinositides
    • Dowler, S., R. A. Currie, C. P. Downes, and D. R. Alessi. 1999. DAPP1: A dual adaptor for phosphotyrosine and 3-phosphoinositides. Biochem. J. 342: 7-12.
    • (1999) Biochem. J. , vol.342 , pp. 7-12
    • Dowler, S.1    Currie, R.A.2    Downes, C.P.3    Alessi, D.R.4
  • 2
    • 0033603214 scopus 로고    scopus 로고
    • Phosphoinositide binding domains: Embracing 3-phosphate
    • Fruman, D. A., L. E. Rameh, and L. C. Cantley. 1999. Phosphoinositide binding domains: Embracing 3-phosphate. Cell 97:817-820.
    • (1999) Cell , vol.97 , pp. 817-820
    • Fruman, D.A.1    Rameh, L.E.2    Cantley, L.C.3
  • 3
    • 0033582303 scopus 로고    scopus 로고
    • Real-time visualization of PH domain-dependent translocation of phospholipase C-δ1 in renal epithelial cells (MDCK): Response to hypoosmotic stress
    • Fujii, M., M. Ohtsubo, T. Ogawa, H. Kamata, H. Hirata, and H. Yagisawa. 1999. Real-time visualization of PH domain-dependent translocation of phospholipase C-δ1 in renal epithelial cells (MDCK): Response to hypoosmotic stress. Biochem. Biophys. Res. Commun. 254:284-291.
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 284-291
    • Fujii, M.1    Ohtsubo, M.2    Ogawa, T.3    Kamata, H.4    Hirata, H.5    Yagisawa, H.6
  • 4
    • 0034931142 scopus 로고    scopus 로고
    • Sprouty4 acts in vivo as a feedback-induced antagonist of FGF signaling in zebrafish
    • Fürthauer, M., F. Reifers, M. Brand, B. Thisse, and C. Thisse. 2001. Sprouty4 acts in vivo as a feedback-induced antagonist of FGF signaling in zebrafish. Development 128:2175-2186.
    • (2001) Development , vol.128 , pp. 2175-2186
    • Fürthauer, M.1    Reifers, F.2    Brand, M.3    Thisse, B.4    Thisse, C.5
  • 5
    • 0032559228 scopus 로고    scopus 로고
    • Sprouty encodes a novel antagonist of FGF signaling that patterns apical branching of the Drosophila airways
    • Hacohen, N., S. Kramer, D. Sutherland, Y. Hiromi, and M. A. Krasnow. 1998. Sprouty encodes a novel antagonist of FGF signaling that patterns apical branching of the Drosophila airways. Cell 92:253-263.
    • (1998) Cell , vol.92 , pp. 253-263
    • Hacohen, N.1    Kramer, S.2    Sutherland, D.3    Hiromi, Y.4    Krasnow, M.A.5
  • 7
    • 0035809919 scopus 로고    scopus 로고
    • Mammalian Sprouty-1 and -2 are membrane-anchored phosphoprotein inhibitors of growth factor signaling in endothelial cells
    • Impagnatiello, M. A., S. Weitzer, G. Gannon, A. Compagni, M. Cotton, and G. Christofori. 2001. Mammalian Sprouty-1 and -2 are membrane-anchored phosphoprotein inhibitors of growth factor signaling in endothelial cells. J. Cell Biol. 152:1087-1098.
    • (2001) J. Cell Biol. , vol.152 , pp. 1087-1098
    • Impagnatiello, M.A.1    Weitzer, S.2    Gannon, G.3    Compagni, A.4    Cotton, M.5    Christofori, G.6
  • 8
    • 0035134328 scopus 로고    scopus 로고
    • Role of the ENTH domain in phosphatidylinositol 4,5-bisphosphate binding and endocytosis
    • Itoh, T., S. Koshiba, T. Kigawa, A. Kikuchi, S. Yokoyama, and T. Takenawa. 2001. Role of the ENTH domain in phosphatidylinositol 4,5-bisphosphate binding and endocytosis. Science 291:1047-1051.
    • (2001) Science , vol.291 , pp. 1047-1051
    • Itoh, T.1    Koshiba, S.2    Kigawa, T.3    Kikuchi, A.4    Yokoyama, S.5    Takenawa, T.6
  • 10
    • 0344417107 scopus 로고    scopus 로고
    • Rac homologues and compartmentalized phosphatidylinositol 4,5-bisphosphate act in a common pathway to regulate polar pollen tube growth
    • Kost, B., E. Lemichez, P. Spielhofer, Y. Hong, K. Tolias, C. Carpenter, and N. H. Chua. 1999. Rac homologues and compartmentalized phosphatidylinositol 4, 5-bisphosphate act in a common pathway to regulate polar pollen tube growth. J. Cell Biol. 145:317-330.
    • (1999) J. Cell Biol. , vol.145 , pp. 317-330
    • Kost, B.1    Lemichez, E.2    Spielhofer, P.3    Hong, Y.4    Tolias, K.5    Carpenter, C.6    Chua, N.H.7
  • 11
    • 0034693130 scopus 로고    scopus 로고
    • Sprouty proteins are targeted to membrane ruffles upon growth factor receptor tyrosine kinase activation: Identification of a novel translocation domain
    • Lim, J., E. S. Wong, S. H. Ong, P. Yusoff, B. C. Low, and G. R. Guy. 2000. Sprouty proteins are targeted to membrane ruffles upon growth factor receptor tyrosine kinase activation: Identification of a novel translocation domain. J. Biol. Chem. 275:32837-32845.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32837-32845
    • Lim, J.1    Wong, E.S.2    Ong, S.H.3    Yusoff, P.4    Low, B.C.5    Guy, G.R.6
  • 12
    • 0035056454 scopus 로고    scopus 로고
    • Evidence that Sprouty2 functions as an inhibitor of mouse embryonic lung growth and morphogenesis
    • Mailleux, A. A., D. Tefft, D. Ndiaye, N. Itoh, J. P. Thiery, D. Warburton, and S. Bellusci. 2001. Evidence that Sprouty2 functions as an inhibitor of mouse embryonic lung growth and morphogenesis. Mech. Dev. 102:81-94.
    • (2001) Mech. Dev. , vol.102 , pp. 81-94
    • Mailleux, A.A.1    Tefft, D.2    Ndiaye, D.3    Itoh, N.4    Thiery, J.P.5    Warburton, D.6    Bellusci, S.7
  • 13
    • 0032719944 scopus 로고    scopus 로고
    • Vertebrate Sprouty genes are induced by FGF signaling and can cause chondrodysplasia when overexpressed
    • Minowada, G., L. A. Jarvis, C. L. Chi, A. Neubuser, X. Sun, N. Hacohen, M. A. Krasnow, and G. R. Martin. 1999. Vertebrate Sprouty genes are induced by FGF signaling and can cause chondrodysplasia when overexpressed. Development 126:4465-4475.
    • (1999) Development , vol.126 , pp. 4465-4475
    • Minowada, G.1    Jarvis, L.A.2    Chi, C.L.3    Neubuser, A.4    Sun, X.5    Hacohen, N.6    Krasnow, M.A.7    Martin, G.R.8
  • 14
    • 0035478249 scopus 로고    scopus 로고
    • Structural properties of lipid-binding sites in cytoskeletal proteins
    • Niggli, V. 2001. Structural properties of lipid-binding sites in cytoskeletal proteins. Trends Biochem. Sci. 26:604-611.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 604-611
    • Niggli, V.1
  • 15
    • 0032498538 scopus 로고    scopus 로고
    • Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells
    • Oancea, E., M. N. Teruel, A. F. G. Quest, and T. Meyer. 1998. Green fluorescent protein (GFP)-tagged cysteine-rich domains from protein kinase C as fluorescent indicators for diacylglycerol signaling in living cells. J. Cell Biol. 140:485-498.
    • (1998) J. Cell Biol. , vol.140 , pp. 485-498
    • Oancea, E.1    Teruel, M.N.2    Quest, A.F.G.3    Meyer, T.4
  • 17
    • 0029795963 scopus 로고    scopus 로고
    • Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase
    • Radhakrishna, H., R. D. Klausner, and J. G. Donaldson. 1996. Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase. J. Cell Biol. 134:935-947.
    • (1996) J. Cell Biol. , vol.134 , pp. 935-947
    • Radhakrishna, H.1    Klausner, R.D.2    Donaldson, J.G.3
  • 18
    • 0034695461 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion
    • Raucher, D., T. Stauffer, W. Chen, K. Shen, S. Guo, J. D. York, M. P. Sheetz, and T. Meyer. 2000. Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion. Cell 100:221-228.
    • (2000) Cell , vol.100 , pp. 221-228
    • Raucher, D.1    Stauffer, T.2    Chen, W.3    Shen, K.4    Guo, S.5    York, J.D.6    Sheetz, M.P.7    Meyer, T.8
  • 19
    • 0034604717 scopus 로고    scopus 로고
    • The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras
    • Rizzo, M. A., K. Shome, S. C. Watkins, and G. Romero. 2000. The recruitment of Raf-1 to membranes is mediated by direct interaction with phosphatidic acid and is independent of association with Ras. J. Biol. Chem. 275:23911-23918.
    • (2000) J. Biol. Chem. , vol.275 , pp. 23911-23918
    • Rizzo, M.A.1    Shome, K.2    Watkins, S.C.3    Romero, G.4
  • 20
    • 0035817625 scopus 로고    scopus 로고
    • Activation of ARF6 by ARNO stimulates epithelial cell migration through downstream activation of both Rac1 and phospholipase D
    • Santy, L. C., and J. E. Casanova. 2001. Activation of ARF6 by ARNO stimulates epithelial cell migration through downstream activation of both Rac1 and phospholipase D. J. Cell Biol. 154:599-610.
    • (2001) J. Cell Biol. , vol.154 , pp. 599-610
    • Santy, L.C.1    Casanova, J.E.2
  • 22
    • 0032829333 scopus 로고    scopus 로고
    • Distinct roles of Profilin in cell morphological changes: Microspikes, membrane ruffles, stress fibers, and cytokinesis
    • Suetsugu, S., H. Miki, and T. Takenawa. 1999. Distinct roles of Profilin in cell morphological changes: Microspikes, membrane ruffles, stress fibers, and cytokinesis. FEBS Lett. 457:470-474.
    • (1999) FEBS Lett. , vol.457 , pp. 470-474
    • Suetsugu, S.1    Miki, H.2    Takenawa, T.3
  • 23
    • 0032538888 scopus 로고    scopus 로고
    • The essential role of Profilin in the assembly of actin for microspike formation
    • Suetsugu, S., H. Miki, and T. Takenawa. 1998. The essential role of Profilin in the assembly of actin for microspike formation. EMBO J. 17:6516-6526.
    • (1998) EMBO J. , vol.17 , pp. 6516-6526
    • Suetsugu, S.1    Miki, H.2    Takenawa, T.3
  • 24
    • 0033231171 scopus 로고    scopus 로고
    • Progress in protrusion: The tell-tale scar
    • Svitkina, T. M., and G. G. Borisy. 1999. Progress in protrusion: The tell-tale scar. Trends Biochem. Sci. 24:432-436.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 432-436
    • Svitkina, T.M.1    Borisy, G.G.2
  • 25
    • 0034659468 scopus 로고    scopus 로고
    • Dynamics of phosphatidylinositol 4,5-bisphosphate in actin-rich structures
    • Tall, E. G., I. Spector, S. N. Pentyala, I. Bitter, and M. J. Rebeechi. 2000. Dynamics of phosphatidylinositol 4,5-bisphosphate in actin-rich structures. Curr. Biol. 10:743-746.
    • (2000) Curr. Biol. , vol.10 , pp. 743-746
    • Tall, E.G.1    Spector, I.2    Pentyala, S.N.3    Bitter, I.4    Rebeechi, M.J.5
  • 26
    • 0032053708 scopus 로고    scopus 로고
    • The synthesis and cellular roles of phosphatidylinositol 4,5-bisphosphate
    • Toker, A. 1998. The synthesis and cellular roles of phosphatidylinositol 4,5-bisphosphate. Curr. Opin. Cell Biol. 10:254-261.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 254-261
    • Toker, A.1
  • 27
    • 0034628109 scopus 로고    scopus 로고
    • Type I alpha phosphatidylinositol 4-phosphate 5-kinase mediates Rac-dependent actin assembly
    • Tolias, K. F., J. H. Hartwig, H. Ishihara, Y. Shibasaki, L. C. Cantley, and C. L. Carpenter. 2000. Type I alpha phosphatidylinositol 4-phosphate 5-kinase mediates Rac-dependent actin assembly. Curr. Biol. 10:153-156.
    • (2000) Curr. Biol. , vol.10 , pp. 153-156
    • Tolias, K.F.1    Hartwig, J.H.2    Ishihara, H.3    Shibasaki, Y.4    Cantley, L.C.5    Carpenter, C.L.6
  • 28
    • 0032547744 scopus 로고    scopus 로고
    • 3H]inositol-labeled phosphoinositide pools
    • 3H]inositol-labeled phosphoinositide pools. J. Cell Biol. 143:501-510.
    • (1998) J. Cell Biol. , vol.143 , pp. 501-510
    • Várnai, P.1    Balla, T.2
  • 30
    • 0035937167 scopus 로고    scopus 로고
    • Evidence for direct interaction between Sprouty and Cb1
    • Wong, E. S. M., J. Lim, B. C. Low, Q. Chen, and G. R. Guy. 2001. Evidence for direct interaction between Sprouty and Cb1. J. Biol. Chem. 276:5866-5875.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5866-5875
    • Wong, E.S.M.1    Lim, J.2    Low, B.C.3    Chen, Q.4    Guy, G.R.5
  • 31
    • 0035893581 scopus 로고    scopus 로고
    • The Phox homology (PX) domain, a new player in phosphoinositide signaling
    • Xu, Y., L. F. Seet, B. Hanson, and W. Hong. 2001. The Phox homology (PX) domain, a new player in phosphoinositide signaling. Biochem. J. 360:513-530.
    • (2001) Biochem. J. , vol.360 , pp. 513-530
    • Xu, Y.1    Seet, L.F.2    Hanson, B.3    Hong, W.4
  • 32
    • 0035933734 scopus 로고    scopus 로고
    • The C terminus of Sprouty is important for modulation of cellular migration and proliferation
    • Yigzaw, Y., L. Cartin, S. Pierre, K. Scholich, and T. B. Patel. 2001. The C terminus of Sprouty is important for modulation of cellular migration and proliferation. J. Biol. Chem. 276:22742-22747.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22742-22747
    • Yigzaw, Y.1    Cartin, L.2    Pierre, S.3    Scholich, K.4    Patel, T.B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.