메뉴 건너뛰기




Volumn 5, Issue 11, 2003, Pages 1016-1022

Production of PtdInsP3 at endomembranes is triggered by receptor endocytosis

Author keywords

[No Author keywords available]

Indexed keywords

LIGAND; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PROTEIN TYROSINE KINASE;

EID: 0242441598     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1054     Document Type: Article
Times cited : (168)

References (30)
  • 1
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L. C. The phosphoinositide 3-kinase pathway. Science 296, 1655-1657 (2002).
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 2
    • 0034677631 scopus 로고    scopus 로고
    • 3: Complex roles at the cell surface
    • 3: complex roles at the cell surface. Cell 100, 603-606 (2000).
    • (2000) Cell , vol.100 , pp. 603-606
    • Czech, M.P.1
  • 3
    • 0030884103 scopus 로고    scopus 로고
    • PKB/Akt: Connecting phosphoinositide 3-kinase to cell survival and beyond
    • Marte, B. M. & Downward, J. PKB/Akt: connecting phosphoinositide 3-kinase to cell survival and beyond. Trends Biochem. Sci. 22, 355-358 (1997).
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 355-358
    • Marte, B.M.1    Downward, J.2
  • 4
    • 0032497832 scopus 로고    scopus 로고
    • Structure and function of phosphoinositide 3-kinases
    • 1436
    • Wymann, M. P. & Pirola, L. Structure and function of phosphoinositide 3-kinases. Biochim. Biophys. Acta 1436, 127-150 (1998).
    • (1998) Biochim. Biophys. Acta , pp. 127-150
    • Wymann, M.P.1    Pirola, L.2
  • 5
    • 0345561543 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase-dependent membrane association of the Bruton's tyrosine kinase pleckstrin homology domain visualized in single living cells
    • Varnai, P., Rother, K. I. & Balla, T. Phosphatidylinositol 3-kinase-dependent membrane association of the Bruton's tyrosine kinase pleckstrin homology domain visualized in single living cells. J. Biol. Chem. 274, 10983-10989 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 10983-10989
    • Varnai, P.1    Rother, K.I.2    Balla, T.3
  • 6
    • 0032189234 scopus 로고    scopus 로고
    • Nerve growth factor- and epidermal growth factor-stimulated translocation of the ADP ribosylation factor-exchange factor GRP1 to the plasma membrane of PC12 cells requires phosphatidylinositol 3-kinase and the GRP1 pleckstrin homology domain
    • Venkateswarlu, K., Gunn-Moore, F., Tavare, J. M. & Cullen, P. J. Nerve growth factor- and epidermal growth factor-stimulated translocation of the ADP ribosylation factor-exchange factor GRP1 to the plasma membrane of PC12 cells requires phosphatidylinositol 3-kinase and the GRP1 pleckstrin homology domain. Biochem. J. 335, 139-146 (1998).
    • (1998) Biochem. J. , vol.335 , pp. 139-146
    • Venkateswarlu, K.1    Gunn-Moore, F.2    Tavare, J.M.3    Cullen, P.J.4
  • 7
    • 0032499031 scopus 로고    scopus 로고
    • Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase
    • Venkateswarlu, K., Oatey, P. B., Tavare, J. M. & Cullen, P. J. Insulin-dependent translocation of ARNO to the plasma membrane of adipocytes requires phosphatidylinositol 3-kinase. Curr. Biol. 8, 463-466 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 463-466
    • Venkateswarlu, K.1    Oatey, P.B.2    Tavare, J.M.3    Cullen, P.J.4
  • 8
    • 0033594403 scopus 로고    scopus 로고
    • Akt/PKB localisation and 3′ phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction
    • Watton, S. J. & Downward, J. Akt/PKB localisation and 3′ phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction, Curr. Biol. 9, 433-436 (1999).
    • (1999) Curr. Biol. , vol.9 , pp. 433-436
    • Watton, S.J.1    Downward, J.2
  • 9
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
    • Miyawaki, A. & Tsien, R. Y. Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein. Method. Enzymol. 327, 472-500 (2000).
    • (2000) Method. Enzymol. , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 10
    • 0034671963 scopus 로고    scopus 로고
    • Fluorescent indicators for cyclic GMP based on cyclic GMP-dependent protein kinase Iα and green fluorescent proteins
    • Sato, M., Hida, N., Ozawa, T. & Umezawa, Y. Fluorescent indicators for cyclic GMP based on cyclic GMP-dependent protein kinase Iα and green fluorescent proteins. Anal. Chem. 72, 5918-5924 (2000 ).
    • (2000) Anal. Chem. , vol.72 , pp. 5918-5924
    • Sato, M.1    Hida, N.2    Ozawa, T.3    Umezawa, Y.4
  • 11
    • 0036196296 scopus 로고    scopus 로고
    • Fluorescent indicators for imaging protein phosphorylation in single living cells
    • Sato, M., Ozawa, T., Inukai, K., Asano, T. & Umezawa, Y. Fluorescent indicators for imaging protein phosphorylation in single living cells. Nature Biotechnol. 20, 287-294 (2002).
    • (2002) Nature Biotechnol. , vol.20 , pp. 287-294
    • Sato, M.1    Ozawa, T.2    Inukai, K.3    Asano, T.4    Umezawa, Y.5
  • 12
    • 0025755941 scopus 로고
    • A model peptide with enhanced helicity
    • Merutka, G., Shalongo, W. & Stellwagen, E. A model peptide with enhanced helicity. Biochemistry 30, 4245-4248 (1991).
    • (1991) Biochemistry , vol.30 , pp. 4245-4248
    • Merutka, G.1    Shalongo, W.2    Stellwagen, E.3
  • 13
    • 0030250003 scopus 로고    scopus 로고
    • Regulation of cellular signaling by fatty acid acylation and prenylation of signal transduction proteins
    • Resh, M. D. Regulation of cellular signaling by fatty acid acylation and prenylation of signal transduction proteins. Cell. Signal. 8, 403-412 (1996).
    • (1996) Cell. Signal. , vol.8 , pp. 403-412
    • Resh, M.D.1
  • 14
    • 0033538559 scopus 로고    scopus 로고
    • Endomembrane trafficking of Ras: The CAAX motif targets proteins to the ER and Golgi
    • Choy, E. et al. Endomembrane trafficking of Ras: the CAAX motif targets proteins to the ER and Golgi. Cell 98, 69-80 (1999).
    • (1999) Cell , vol.98 , pp. 69-80
    • Choy, E.1
  • 15
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 103, 211-225 (2000).
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 16
    • 0033572662 scopus 로고    scopus 로고
    • The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositide-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-triphosphate in vivo
    • Gray, A., Kaay, J.V.D. & Downes, C. P. The pleckstrin homology domains of protein kinase B and GRP1 (general receptor for phosphoinositide-1) are sensitive and selective probes for the cellular detection of phosphatidylinositol 3,4-bisphosphate and/or phosphatidylinositol 3,4,5-triphosphate in vivo. Biochem. J. 344, 929-936 (1999).
    • (1999) Biochem. J. , vol.344 , pp. 929-936
    • Gray, A.1    Kaay, J.V.D.2    Downes, C.P.3
  • 17
    • 0032805160 scopus 로고    scopus 로고
    • EGF- and NGF-stimulated translocation of cytohensine-1 to the plasma membrane of PC12 cells requires PI 3-kinase activation and a functional cytohensin-1 PH domain
    • Venkateswarlu, K., Gunn-Moore, F., Tavare, J. M. & Cullen, P. J. EGF- and NGF-stimulated translocation of cytohensine-1 to the plasma membrane of PC12 cells requires PI 3-kinase activation and a functional cytohensin-1 PH domain. J. Cell Sci. 112, 1957-1965 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 1957-1965
    • Venkateswarlu, K.1    Gunn-Moore, F.2    Tavare, J.M.3    Cullen, P.J.4
  • 18
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • Vieira, A. V., Lamaze, C. & Schmid, S. L. Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 274, 2086-2089 (1996).
    • (1996) Science , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 19
    • 0034605038 scopus 로고    scopus 로고
    • Molecular links between endocytosis and the actin cytoskeleton
    • Qualmann, B., Kessels, M. M. & Kelly, R. B. Molecular links between endocytosis and the actin cytoskeleton. J. Cell Biol. 150, F111-F116 (2000).
    • (2000) J. Cell Biol. , vol.150
    • Qualmann, B.1    Kessels, M.M.2    Kelly, R.B.3
  • 20
    • 0026584285 scopus 로고
    • The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence
    • Frangioni, J. V., Beahm, P. H., Shifrin, V., Jost, C, A. & Neel, B. G. The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. Cell 68, 545-560 (1992).
    • (1992) Cell , vol.68 , pp. 545-560
    • Frangioni, J.V.1    Beahm, P.H.2    Shifrin, V.3    Jost, C.A.4    Neel, B.G.5
  • 21
    • 0036500994 scopus 로고    scopus 로고
    • Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum
    • Haj, F. G., Verveer, P. J., Squire, A., Neel, B. G. & Bastiaens, P. I. H. Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum. Science 295, 1708-1711 (2002).
    • (2002) Science , vol.295 , pp. 1708-1711
    • Haj, F.G.1    Verveer, P.J.2    Squire, A.3    Neel, B.G.4    Bastiaens, P.I.H.5
  • 22
    • 0034011765 scopus 로고    scopus 로고
    • Regulation of signal transduction by endocytosis
    • Ceresa, B. C. & Schmid, S. L. Regulation of signal transduction by endocytosis. Curr. Opin. Cell Biol. 12, 204-210 (2000).
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 204-210
    • Ceresa, B.C.1    Schmid, S.L.2
  • 23
    • 0037144542 scopus 로고    scopus 로고
    • β1/β2-adrenergic receptor heterodimerization regulates β2-adrenergic receptor internalization and ERK signaling efficacy
    • Lavoie, C. et al. β1/β2-adrenergic receptor heterodimerization regulates β2-adrenergic receptor internalization and ERK signaling efficacy. J. Biol. Chem. 277, 35402-35410 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 35402-35410
    • Lavoie, C.1
  • 25
    • 0037040278 scopus 로고    scopus 로고
    • Localization of endothelial nitric-oxide synthase phosphorylated on serine 1179 and nitric oxide in Golgi and plasma membrane defines the existence of two pools of active enzyme
    • Fulton, D. et al. Localization of endothelial nitric-oxide synthase phosphorylated on serine 1179 and nitric oxide in Golgi and plasma membrane defines the existence of two pools of active enzyme. J. Biol. Chem. 277, 4277-4284 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 4277-4284
    • Fulton, D.1
  • 26
    • 0042733215 scopus 로고    scopus 로고
    • Fluorescent indicators for Akt/Protein Kinase B and dynamics of Akt activity visualized in living cells
    • Sasaki, K., Sato, M. & Umezawa, Y. Fluorescent indicators for Akt/Protein Kinase B and dynamics of Akt activity visualized in living cells. J. Biol. Chem. 278, 30945-30951 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 30945-30951
    • Sasaki, K.1    Sato, M.2    Umezawa, Y.3
  • 27
    • 0033537768 scopus 로고    scopus 로고
    • 2+-induced apoptosis through calcineurin dephosphorylation of BAD
    • 2+-induced apoptosis through calcineurin dephosphorylation of BAD. Science 284, 339-343 (1999).
    • (1999) Science , vol.284 , pp. 339-343
    • Wang, H.-G.1
  • 28
    • 0028979464 scopus 로고
    • Crystal structure of the Cys2 activator-binding domain of prortein kinase C δ in complex with phorbol ester
    • Zhang, G., Kazanietz, M. G., Blumberg, P. M. & Hurley, J. H. Crystal structure of the Cys2 activator-binding domain of prortein kinase C δ in complex with phorbol ester. Cell 81, 917-924 (1995).
    • (1995) Cell , vol.81 , pp. 917-924
    • Zhang, G.1    Kazanietz, M.G.2    Blumberg, P.M.3    Hurley, J.H.4
  • 29
    • 0035977098 scopus 로고    scopus 로고
    • Recognition of phosphatidylinositol 3-phosphate
    • Misra, S., Miller, G. J. & Hurley, J. H. Recognition of phosphatidylinositol 3-phosphate. Cell 107, 559-562 (2001).
    • (2001) Cell , vol.107 , pp. 559-562
    • Misra, S.1    Miller, G.J.2    Hurley, J.H.3
  • 30
    • 0033021116 scopus 로고    scopus 로고
    • Characterisation of a plant 3-phosphoinositide-dependent protein kinase-1 homologue which contains a pleckstrin homology domain
    • Deak, M., Casamayor, A., Currie, R. A., Downes, C. P. & Alessi D. R. Characterisation of a plant 3-phosphoinositide-dependent protein kinase-1 homologue which contains a pleckstrin homology domain. FEBS Lett. 451, 220-226 (1999).
    • (1999) FEBS Lett. , vol.451 , pp. 220-226
    • Deak, M.1    Casamayor, A.2    Currie, R.A.3    Downes, C.P.4    Alessi, D.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.