메뉴 건너뛰기




Volumn 6, Issue 279, 2013, Pages

AKT facilitates EGFR trafficking and degradation by phosphorylating and activating PIKfyve

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHATIDYLINOSITOL 3 PHOSPHATE 5 KINASE; PLATELET DERIVED GROWTH FACTOR RECEPTOR; PROTEIN KINASE; PROTEIN KINASE B; S6 KINASE; UNCLASSIFIED DRUG; PHOSPHATIDYLINOSITOL 3 KINASE; PIKFYVE PROTEIN, HUMAN;

EID: 84879987829     PISSN: 19450877     EISSN: 19379145     Source Type: Journal    
DOI: 10.1126/scisignal.2004015     Document Type: Article
Times cited : (84)

References (72)
  • 2
    • 34250216633 scopus 로고    scopus 로고
    • Mutational activation of ErbB family receptor tyrosine kinases: Insights into mechanisms of signal transduction and tumorigenesis
    • D. J. Riese II, R. M. Gallo, J. Settleman, Mutational activation of ErbB family receptor tyrosine kinases: Insights into mechanisms of signal transduction and tumorigenesis. Bioessays 29, 558-565 (2007).
    • (2007) Bioessays. , vol.29 , pp. 558-565
    • Riese, I.I.D.J.1    Gallo, R.M.2    Settleman, J.3
  • 3
    • 79958026380 scopus 로고    scopus 로고
    • The Ras-ERK and PI3K-mTOR pathways: Cross-talk and compensation
    • M. C. Mendoza, E. E. Er, J. Blenis, The Ras-ERK and PI3K-mTOR pathways: Cross-talk and compensation. Trends Biochem. Sci. 36, 320-328 (2011).
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 320-328
    • Mendoza, M.C.1    Er, E.E.2    Blenis, J.3
  • 6
    • 42949092018 scopus 로고    scopus 로고
    • The endosomal protein Appl1 mediates Akt substrate specificity and cell survival in vertebrate development
    • A. Schenck, L. Goto-Silva, C. Collinet, M. Rhinn, A. Giner, B. Habermann, M. Brand, M. Zerial, The endosomal protein Appl1 mediates Akt substrate specificity and cell survival in vertebrate development. Cell 133, 486-497 (2008).
    • (2008) Cell. , vol.133 , pp. 486-497
    • Schenck, A.1    Goto-Silva, L.2    Collinet, C.3    Rhinn, M.4    Giner, A.5    Habermann, B.6    Brand, M.7    Zerial, M.8
  • 7
    • 62549151303 scopus 로고    scopus 로고
    • A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes
    • R. Zoncu, R. M. Perera, D. M. Balkin, M. Pirruccello, D. Toomre, P. De Camilli, A phosphoinositide switch controls the maturation and signaling properties of APPL endosomes. Cell 136, 1110-1121 (2009).
    • (2009) Cell. , vol.136 , pp. 1110-1121
    • Zoncu, R.1    Perera, R.M.2    Balkin, D.M.3    Pirruccello, M.4    Toomre, D.5    De Camilli, P.6
  • 8
    • 77950460037 scopus 로고    scopus 로고
    • Spatial control ofEGF receptor activation by reversible dimerization on living cells
    • I. Chung, R. Akita, R. Vandlen, D. Toomre, J.Schlessinger, I.Mellman, Spatial control ofEGF receptor activation by reversible dimerization on living cells. Nature 464, 783-787 (2010).
    • (2010) Nature. , vol.464 , pp. 783-787
    • Chung, I.1    Akita, R.2    Vandlen, R.3    Toomre, D.4    Schlessinger, J.5    Mellman, I.6
  • 9
    • 77953167957 scopus 로고    scopus 로고
    • Multiple mechanisms collectively regulate clathrin-mediated endocytosis of the epidermal growth factor receptor
    • L. K. Goh, F. Huang, W. Kim, S. Gygi, A. Sorkin, Multiple mechanisms collectively regulate clathrin-mediated endocytosis of the epidermal growth factor receptor. J. Cell Biol. 189, 871-883 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 871-883
    • Goh, L.K.1    Huang, F.2    Kim, W.3    Gygi, S.4    Sorkin, A.5
  • 11
    • 33845757583 scopus 로고    scopus 로고
    • Get off my back! Rapid receptor internalization through circular dorsal ruffles
    • J. D. Orth, M. A. McNiven, Get off my back! Rapid receptor internalization through circular dorsal ruffles. Cancer Res. 66, 11094-11096 (2006).
    • (2006) Cancer Res. , vol.66 , pp. 11094-11096
    • Orth, J.D.1    McNiven, M.A.2
  • 12
    • 33644764063 scopus 로고    scopus 로고
    • Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes
    • M. Lakadamyali, M. J. Rust, X. Zhuang, Ligands for clathrin-mediated endocytosis are differentially sorted into distinct populations of early endosomes. Cell 124, 997-1009 (2006).
    • (2006) Cell. , vol.124 , pp. 997-1009
    • Lakadamyali, M.1    Rust, M.J.2    Zhuang, X.3
  • 14
    • 75749096347 scopus 로고    scopus 로고
    • The endocytic matrix
    • G. Scita, P. P. Di Fiore, The endocytic matrix. Nature 463, 464-473 (2010).
    • (2010) Nature. , vol.463 , pp. 464-473
    • Scita, G.1    Di Fiore, P.P.2
  • 15
    • 77649274212 scopus 로고    scopus 로고
    • Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction
    • E. R. Eden, I. J. White, A. Tsapara, C. E. Futter, Membrane contacts between endosomes and ER provide sites for PTP1B-epidermal growth factor receptor interaction. Nat. Cell Biol. 12, 267-272 (2010).
    • (2010) Nat. Cell Biol. , vol.12 , pp. 267-272
    • Eden, E.R.1    White, I.J.2    Tsapara, A.3    Futter, C.E.4
  • 16
    • 0036500994 scopus 로고    scopus 로고
    • Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum
    • F. G. Haj, P. J. Verveer, A. Squire, B. G. Neel, P. I. Bastiaens, 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.5
  • 18
    • 83255194137 scopus 로고    scopus 로고
    • Phosphatidylinositol-3,5-bisphosphate: No longer the poor PIP2
    • C. Y. Ho, T. A. Alghamdi, R. J. Botelho, Phosphatidylinositol-3,5- bisphosphate: No longer the poor PIP2. Traffic 13, 1-8 (2012).
    • (2012) Traffic. , vol.13 , pp. 1-8
    • Ho, C.Y.1    Alghamdi, T.A.2    Botelho, R.J.3
  • 19
    • 0032217266 scopus 로고    scopus 로고
    • Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body
    • G. Odorizzi, M. Babst, S. D. Emr, Fab1p PtdIns(3)P 5-kinase function essential for protein sorting in the multivesicular body. Cell 95, 847-858 (1998).
    • (1998) Cell. , vol.95 , pp. 847-858
    • Odorizzi, G.1    Babst, M.2    Emr, S.D.3
  • 20
    • 34548221502 scopus 로고    scopus 로고
    • Core protein machinery for mammalian phosphatidylinositol 3,5-bisphosphate synthesis and turnover that regulates the progression of endosomal transport. Novel Sac phosphatase joins the ArPIKfyve-PIKfyve complex
    • D. Sbrissa, O. C. Ikonomov, Z. Fu, T. Ijuin, J. Gruenberg, T. Takenawa, A. Shisheva, Core protein machinery for mammalian phosphatidylinositol 3,5-bisphosphate synthesis and turnover that regulates the progression of endosomal transport. Novel Sac phosphatase joins the ArPIKfyve-PIKfyve complex. J. Biol. Chem. 282, 23878-23891 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 23878-23891
    • Sbrissa, D.1    Ikonomov, O.C.2    Fu, Z.3    Ijuin, T.4    Gruenberg, J.5    Takenawa, T.6    Shisheva, A.7
  • 21
    • 0028351218 scopus 로고
    • Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites
    • M. Joly, A. Kazlauskas, F. S. Fay, S. Corvera, Disruption of PDGF receptor trafficking by mutation of its PI-3 kinase binding sites. Science 263, 684-687 (1994).
    • (1994) Science. , vol.263 , pp. 684-687
    • Joly, M.1    Kazlauskas, A.2    Fay, F.S.3    Corvera, S.4
  • 23
    • 0032517624 scopus 로고    scopus 로고
    • Distinct roles for the p110a and hVPS34 phosphatidylinositol 3′-kinases in vesicular trafficking, regulation of the actin cytoskeleton, and mitogenesis
    • U. Siddhanta, J. McIlroy, A. Shah, Y. Zhang, J. M. Backer, Distinct roles for the p110a and hVPS34 phosphatidylinositol 3′-kinases in vesicular trafficking, regulation of the actin cytoskeleton, and mitogenesis. J. Cell Biol. 143, 1647-1659 (1998).
    • (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
  • 24
    • 0029933270 scopus 로고    scopus 로고
    • Wortmannin alters the transferrin receptor endocytic pathway in vivo and in vitro
    • D. J. Spiro, W. Boll, T. Kirchhausen, M. Wessling-Resnick, Wortmannin alters the transferrin receptor endocytic pathway in vivo and in vitro. Mol. Biol. Cell 7, 355-367 (1996).
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 355-367
    • Spiro, D.J.1    Boll, W.2    Kirchhausen, T.3    Wessling-Resnick, M.4
  • 25
    • 67649852605 scopus 로고    scopus 로고
    • Sorting in early endosomes reveals connections to docking- and fusion-associated factors
    • S. V. Barysch, S. Aggarwal, R. Jahn, S. O. Rizzoli, Sorting in early endosomes reveals connections to docking- and fusion-associated factors. Proc. Natl. Acad. Sci. U.S.A. 106, 9697-9702 (2009).
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 9697-9702
    • Barysch, S.V.1    Aggarwal, S.2    Jahn, R.3    Rizzoli, S.O.4
  • 29
    • 37049185280 scopus 로고
    • Amplification and enhanced expression of the epidermal growth factor receptor gene in A431 human carcinoma cells
    • G. T. Merlino, Y. H. Xu, S. Ishii, A. J. Clark, K. Semba, K. Toyoshima, T. Yamamoto, I. Pastan, Amplification and enhanced expression of the epidermal growth factor receptor gene in A431 human carcinoma cells. Science 224, 417-419 (1984).
    • (1984) Science. , vol.224 , pp. 417-419
    • Merlino, G.T.1    Xu, Y.H.2    Ishii, S.3    Clark, A.J.4    Semba, K.5    Toyoshima, K.6    Yamamoto, T.7    Pastan, I.8
  • 30
    • 0021804944 scopus 로고
    • MDA-468, a human breast cancer cell line with a high number of epidermal growth factor (EGF) receptors, has an amplified EGF receptor gene and is growth inhibited by EGF
    • J. Filmus, M. N. Pollak, R. Cailleau, R. N. Buick, MDA-468, a human breast cancer cell line with a high number of epidermal growth factor (EGF) receptors, has an amplified EGF receptor gene and is growth inhibited by EGF. Biochem. Biophys. Res.Commun. 128, 898-905 (1985).
    • (1985) Biochem. Biophys. Res.Commun. , vol.128 , pp. 898-905
    • Filmus, J.1    Pollak, M.N.2    Cailleau, R.3    Buick, R.N.4
  • 34
    • 58849120491 scopus 로고    scopus 로고
    • Role of a novel PH-kinase domain interface in PKB/Akt regulation: Structural mechanism for allosteric inhibition
    • V. Calleja, M. Laguerre, P. J. Parker, B. Larijani, Role of a novel PH-kinase domain interface in PKB/Akt regulation: Structural mechanism for allosteric inhibition. PLoS Biol. 7, e17 (2009).
    • (2009) PLoS Biol. , vol.7
    • Calleja, V.1    Laguerre, M.2    Parker, P.J.3    Larijani, B.4
  • 35
    • 55549088220 scopus 로고    scopus 로고
    • Use of Akt inhibitor and a drug-resistant mutant validates a critical role for protein kinase B/Akt in the insulin-dependent regulation of glucose and system A amino acid uptake
    • C. J. Green, O. Göransson, G. S. Kular, N. R. Leslie, A. Gray, D. R. Alessi, K. Sakamoto, H. S. Hundal, Use of Akt inhibitor and a drug-resistant mutant validates a critical role for protein kinase B/Akt in the insulin-dependent regulation of glucose and system A amino acid uptake. J. Biol. Chem. 283, 27653-27667 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 27653-27667
    • Green, C.J.1    Göransson, O.2    Kular, G.S.3    Leslie, N.R.4    Gray, A.5    Alessi, D.R.6    Sakamoto, K.7    Hundal, H.S.8
  • 38
    • 69249114825 scopus 로고    scopus 로고
    • Sustained receptor stimulation leads to sequestration of recycling endosomes in a classical protein kinase C- and phospholipase D-dependent manner
    • J. Idkowiak-Baldys, A. Baldys, J. R. Raymond, Y. A. Hannun, Sustained receptor stimulation leads to sequestration of recycling endosomes in a classical protein kinase C- and phospholipase D-dependent manner. J. Biol. Chem. 284, 22322-22331 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 22322-22331
    • Idkowiak-Baldys, J.1    Baldys, A.2    Raymond, J.R.3    Hannun, Y.A.4
  • 40
    • 48549088895 scopus 로고    scopus 로고
    • Clathrinmediated internalization is essential for sustained EGFR signaling but dispensable for degradation
    • S. Sigismund, E. Argenzio, D. Tosoni, E. Cavallaro, S. Polo, P. P. Di Fiore, Clathrinmediated internalization is essential for sustained EGFR signaling but dispensable for degradation. Dev. Cell 15, 209-219 (2008).
    • (2008) Dev. Cell. , vol.15 , pp. 209-219
    • Sigismund, S.1    Argenzio, E.2    Tosoni, D.3    Cavallaro, E.4    Polo, S.5    Di Fiore, P.P.6
  • 42
    • 33646019884 scopus 로고    scopus 로고
    • Protein kinase Ba is required for vesicle trafficking and class II presentation of IgA Fc receptor (CD89)-targeted antigen
    • G. A. Lang, M. L. Lang, Protein kinase Ba is required for vesicle trafficking and class II presentation of IgA Fc receptor (CD89)-targeted antigen. J. Immunol. 176, 3987-3994 (2006).
    • (2006) J. Immunol. , vol.176 , pp. 3987-3994
    • Lang, G.A.1    Lang, M.L.2
  • 43
    • 0035340814 scopus 로고    scopus 로고
    • Fca receptor crosslinking causes translocation of phosphatidylinositol- dependent protein kinase 1 and protein kinase Ba to MHC class II peptide-loading-like compartments
    • M. L. Lang, L. Shen, H. Gao, W. F. Cusack, G. A. Lang, W. F. Wade, Fca receptor crosslinking causes translocation of phosphatidylinositol-dependent protein kinase 1 and protein kinase Ba to MHC class II peptide-loading-like compartments. J. Immunol. 166, 5585-5593 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 5585-5593
    • Lang, M.L.1    Shen, L.2    Gao, H.3    Cusack, W.F.4    Lang, G.A.5    Wade, W.F.6
  • 44
    • 61449152986 scopus 로고    scopus 로고
    • Phosphatidylinositol metabolism and membrane fusion
    • D. Poccia, B. Larijani, Phosphatidylinositol metabolism and membrane fusion. Biochem. J. 418, 233-246 (2009).
    • (2009) Biochem. J. , vol.418 , pp. 233-246
    • Poccia, D.1    Larijani, B.2
  • 45
    • 69949143770 scopus 로고    scopus 로고
    • Sac3 is an insulinregulated phosphatidylinositol 3,5-bisphosphate phosphatase: Gain in insulin responsiveness through Sac3 down-regulation in adipocytes
    • O. C. Ikonomov, D. Sbrissa, T. Ijuin, T. Takenawa, A. Shisheva, Sac3 is an insulinregulated phosphatidylinositol 3,5-bisphosphate phosphatase: Gain in insulin responsiveness through Sac3 down-regulation in adipocytes. J. Biol. Chem. 284, 23961-23971 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 23961-23971
    • Ikonomov, O.C.1    Sbrissa, D.2    Ijuin, T.3    Takenawa, T.4    Shisheva, A.5
  • 46
    • 0042622251 scopus 로고    scopus 로고
    • Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs
    • J. C. Obenauer, L. C. Cantley, M. B. Yaffe, Scansite 2.0: Proteome-wide prediction of cell signaling interactions using short sequence motifs. Nucleic Acids Res. 31, 3635- 3641 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3635-3641
    • Obenauer, J.C.1    Cantley, L.C.2    Yaffe, M.B.3
  • 47
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • P. V. Hornbeck, J. M. Kornhauser, S. Tkachev, B. Zhang, E. Skrzypek, B. Murray, V. Latham, M. Sullivan, PhosphoSitePlus: A comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 40, D261-D270 (2012).
    • (2012) Nucleic Acids Res. , vol.40
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6    Latham, V.7    Sullivan, M.8
  • 53
    • 77954930785 scopus 로고    scopus 로고
    • A novel HPLC-based approach makes possible the spatial characterization of cellular PtdIns5P and other phosphoinositides
    • D. Sarkes, L. E. Rameh, A novel HPLC-based approach makes possible the spatial characterization of cellular PtdIns5P and other phosphoinositides. Biochem. J. 428, 375-384 (2010).
    • (2010) Biochem. J. , vol.428 , pp. 375-384
    • Sarkes, D.1    Rameh, L.E.2
  • 56
  • 57
    • 72149091444 scopus 로고    scopus 로고
    • PIKfyve-ArPIKfyve-Sac3 core complex: Contact sites and their consequence for Sac3 phosphatase activity and endocytic membrane homeostasis
    • O. C. Ikonomov, D. Sbrissa, H. Fenner, A. Shisheva, PIKfyve-ArPIKfyve- Sac3 core complex: Contact sites and their consequence for Sac3 phosphatase activity and endocytic membrane homeostasis. J. Biol. Chem. 284, 35794-35806 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 35794-35806
    • Ikonomov, O.C.1    Sbrissa, D.2    Fenner, H.3    Shisheva, A.4
  • 60
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrinmediated endocytosis
    • A. V. Vieira, C. Lamaze, S. L. Schmid, Control of EGF receptor signaling by clathrinmediated endocytosis. Science 274, 2086-2089 (1996).
    • (1996) Science. , vol.274 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 61
    • 0027965262 scopus 로고
    • Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma
    • G. M. Di Guglielmo, P. C. Baass, W. J. Ou, B. I. Posner, J. J. Bergeron, Compartmentalization of SHC, GRB2 and mSOS, and hyperphosphorylation of Raf-1 by EGF but not insulin in liver parenchyma. EMBO J. 13, 4269-4277 (1994).
    • (1994) EMBO J. , vol.13 , pp. 4269-4277
    • Di Guglielmo, G.M.1    Baass, P.C.2    Ou, W.J.3    Posner, B.I.4    Bergeron, J.J.5
  • 62
    • 0042130366 scopus 로고    scopus 로고
    • Stimulation of cell proliferation by endosomal epidermal growth factor receptor as revealed through two distinct phases of signaling
    • S. Pennock, Z. Wang, Stimulation of cell proliferation by endosomal epidermal growth factor receptor as revealed through two distinct phases of signaling. Mol. Cell. Biol. 23, 5803-5815 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5803-5815
    • Pennock, S.1    Wang, Z.2
  • 64
    • 0036899420 scopus 로고    scopus 로고
    • Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction
    • D. Teis, W. Wunderlich, L. A. Huber, Localization of the MP1-MAPK scaffold complex to endosomes is mediated by p14 and required for signal transduction. Dev. Cell 3, 803-814 (2002).
    • (2002) Dev. Cell. , vol.3 , pp. 803-814
    • Teis, D.1    Wunderlich, W.2    Huber, L.A.3
  • 65
    • 0033607633 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Raf by Akt (protein kinase B)
    • S. Zimmermann, K. Moelling, Phosphorylation and regulation of Raf by Akt (protein kinase B). Science 286, 1741-1744 (1999).
    • (1999) Science. , vol.286 , pp. 1741-1744
    • Zimmermann, S.1    Moelling, K.2
  • 68
    • 71949085528 scopus 로고    scopus 로고
    • Aberrant trafficking of NSCLC-associated EGFR mutants through the endocytic recycling pathway promotes interaction with Src
    • B. M. Chung, S. M. Raja, R. J. Clubb, C. Tu, M. George, V. Band, H. Band, Aberrant trafficking of NSCLC-associated EGFR mutants through the endocytic recycling pathway promotes interaction with Src. BMC Cell Biol. 10, 84 (2009).
    • (2009) BMC Cell Biol. , vol.10 , pp. 84
    • Chung, B.M.1    Raja, S.M.2    Clubb, R.J.3    Tu, C.4    George, M.5    Band, V.6    Band, H.7
  • 71
    • 79952114793 scopus 로고    scopus 로고
    • ERK-MAP kinase signaling in the cytoplasm
    • M. C. Mendoza, E. E. Er, J. Blenis, ERK-MAP kinase signaling in the cytoplasm. Methods Mol. Biol. 661, 185-203 (2010).
    • (2010) Methods Mol. Biol. , vol.661 , pp. 185-203
    • Mendoza, M.C.1    Er, E.E.2    Blenis, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.