메뉴 건너뛰기




Volumn 18, Issue 1, 2005, Pages 13-24

PHLPP: A phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; INSULIN; PH DOMAIN LEUCINE RICH REPEAT PROTEIN PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE B; UNCLASSIFIED DRUG;

EID: 15944406764     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.03.008     Document Type: Article
Times cited : (766)

References (40)
  • 2
    • 0032518467 scopus 로고    scopus 로고
    • 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro
    • D.R. Alessi, M.T. Kozlowski, Q.P. Weng, N. Morrice, and J. Avruch 3-Phosphoinositide-dependent protein kinase 1 (PDK1) phosphorylates and activates the p70 S6 kinase in vivo and in vitro Curr. Biol. 8 1998 69 81
    • (1998) Curr. Biol. , vol.8 , pp. 69-81
    • Alessi, D.R.1    Kozlowski, M.T.2    Weng, Q.P.3    Morrice, N.4    Avruch, J.5
  • 3
    • 0029942186 scopus 로고    scopus 로고
    • Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors
    • M. Andjelkovic, T. Jakubowicz, P. Cron, X.F. Ming, J.W. Han, and B.A. Hemmings Activation and phosphorylation of a pleckstrin homology domain containing protein kinase (RAC-PK/PKB) promoted by serum and protein phosphatase inhibitors Proc. Natl. Acad. Sci. USA 93 1996 5699 5704
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5699-5704
    • Andjelkovic, M.1    Jakubowicz, T.2    Cron, P.3    Ming, X.F.4    Han, J.W.5    Hemmings, B.A.6
  • 4
    • 0033565608 scopus 로고    scopus 로고
    • The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation
    • A. Behn-Krappa, and A.C. Newton The hydrophobic phosphorylation motif of conventional protein kinase C is regulated by autophosphorylation Curr. Biol. 9 1999 728 737
    • (1999) Curr. Biol. , vol.9 , pp. 728-737
    • Behn-Krappa, A.1    Newton, A.C.2
  • 5
    • 0034168037 scopus 로고    scopus 로고
    • Protein kinase C-mediated regulation of the cell cycle
    • J.D. Black Protein kinase C-mediated regulation of the cell cycle Front. Biosci. 5 2000 D406 D423
    • (2000) Front. Biosci. , vol.5
    • Black, J.D.1
  • 6
    • 0031021875 scopus 로고    scopus 로고
    • Phosphorylation of protein kinase C-alpha on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase- resistant state
    • F. Bornancin, and P.J. Parker Phosphorylation of protein kinase C-alpha on serine 657 controls the accumulation of active enzyme and contributes to its phosphatase- resistant state J. Biol. Chem. 272 1997 3544 3549
    • (1997) J. Biol. Chem. , vol.272 , pp. 3544-3549
    • Bornancin, F.1    Parker, P.J.2
  • 7
    • 0035872199 scopus 로고    scopus 로고
    • Akt/protein kinase B is constitutively active in non-small cell lung cancer cells and promotes cellular survival and resistance to chemotherapy and radiation
    • J. Brognard, A.S. Clark, Y. Ni, and P.A. Dennis Akt/protein kinase B is constitutively active in non-small cell lung cancer cells and promotes cellular survival and resistance to chemotherapy and radiation Cancer Res. 61 2001 3986 3997
    • (2001) Cancer Res. , vol.61 , pp. 3986-3997
    • Brognard, J.1    Clark, A.S.2    Ni, Y.3    Dennis, P.A.4
  • 9
    • 0024792262 scopus 로고
    • Protein phosphatases come of age
    • P. Cohen, and P.T. Cohen Protein phosphatases come of age J. Biol. Chem. 264 1989 21435 21438
    • (1989) J. Biol. Chem. , vol.264 , pp. 21435-21438
    • Cohen, P.1    Cohen, P.T.2
  • 10
    • 0030465532 scopus 로고    scopus 로고
    • Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 a resolution
    • A.K. Das, N.R. Helps, P.T. Cohen, and D. Barford Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution EMBO J. 15 1996 6798 6809
    • (1996) EMBO J. , vol.15 , pp. 6798-6809
    • Das, A.K.1    Helps, N.R.2    Cohen, P.T.3    Barford, D.4
  • 11
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • S.R. Datta, A. Brunet, and M.E. Greenberg Cellular survival: a play in three Akts Genes Dev. 13 1999 2905 2927
    • (1999) Genes Dev. , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 12
    • 0030875555 scopus 로고    scopus 로고
    • Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C
    • A.S. Edwards, and A.C. Newton Phosphorylation at conserved carboxyl-terminal hydrophobic motif regulates the catalytic and regulatory domains of protein kinase C J. Biol. Chem. 272 1997 18382 18390
    • (1997) J. Biol. Chem. , vol.272 , pp. 18382-18390
    • Edwards, A.S.1    Newton, A.C.2
  • 14
    • 0033575250 scopus 로고    scopus 로고
    • Kinetic analysis of human serine/threonine protein phosphatase 2C alpha
    • C.C. Fjeld, and J.M. Denu Kinetic analysis of human serine/threonine protein phosphatase 2C alpha J. Biol. Chem. 274 1999 20336 20343
    • (1999) J. Biol. Chem. , vol.274 , pp. 20336-20343
    • Fjeld, C.C.1    Denu, J.M.2
  • 15
    • 0030907987 scopus 로고    scopus 로고
    • PI3K: Downstream AKTion blocks apoptosis
    • T.F. Franke, D.R. Kaplan, and L.C. Cantley PI3K: downstream AKTion blocks apoptosis Cell 88 1997 435 437
    • (1997) Cell , vol.88 , pp. 435-437
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3
  • 16
    • 0030728479 scopus 로고    scopus 로고
    • Growth suppression of glioma cells by PTEN requires a functional phosphatase catalytic domain
    • F.B. Furnari, H. Lin, H.S. Huang, and W.K. Cavenee Growth suppression of glioma cells by PTEN requires a functional phosphatase catalytic domain Proc. Natl. Acad. Sci. USA 94 1997 12479 12484
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12479-12484
    • Furnari, F.B.1    Lin, H.2    Huang, H.S.3    Cavenee, W.K.4
  • 17
    • 0035380478 scopus 로고    scopus 로고
    • The carboxyl terminus of protein kinase c provides a switch to regulate its interaction with the phosphoinositide-dependent kinase, pdk-1
    • T. Gao, A. Toker, and A.C. Newton The carboxyl terminus of protein kinase c provides a switch to regulate its interaction with the phosphoinositide- dependent kinase, pdk-1 J. Biol. Chem. 276 2001 19588 19596
    • (2001) J. Biol. Chem. , vol.276 , pp. 19588-19596
    • Gao, T.1    Toker, A.2    Newton, A.C.3
  • 19
    • 1542328927 scopus 로고    scopus 로고
    • Structure, regulation and function of PKB/AKT - A major therapeutic target
    • M. Hanada, J. Feng, and B.A. Hemmings Structure, regulation and function of PKB/AKT - a major therapeutic target Biochim. Biophys. Acta 1697 2004 3 16
    • (2004) Biochim. Biophys. Acta , vol.1697 , pp. 3-16
    • Hanada, M.1    Feng, J.2    Hemmings, B.A.3
  • 20
    • 0035854677 scopus 로고    scopus 로고
    • Insulin-stimulated protein kinase B phosphorylation on Ser-473 is independent of its activity and occurs through a staurosporine-insensitive kinase
    • M.M. Hill, M. Andjelkovic, D.P. Brazil, S. Ferrari, D. Fabbro, and B.A. Hemmings Insulin-stimulated protein kinase B phosphorylation on Ser-473 is independent of its activity and occurs through a staurosporine-insensitive kinase J. Biol. Chem. 276 2001 25643 25646
    • (2001) J. Biol. Chem. , vol.276 , pp. 25643-25646
    • Hill, M.M.1    Andjelkovic, M.2    Brazil, D.P.3    Ferrari, S.4    Fabbro, D.5    Hemmings, B.A.6
  • 21
    • 0032977124 scopus 로고    scopus 로고
    • Frequent co-alterations of TP53, p16/CDKN2A, p14ARF, PTEN tumor suppressor genes in human glioma cell lines
    • N. Ishii, D. Maier, A. Merlo, M. Tada, Y. Sawamura, A.C. Diserens, and E.G. Van Meir Frequent co-alterations of TP53, p16/CDKN2A, p14ARF, PTEN tumor suppressor genes in human glioma cell lines Brain Pathol. 9 1999 469 479
    • (1999) Brain Pathol. , vol.9 , pp. 469-479
    • Ishii, N.1    Maier, D.2    Merlo, A.3    Tada, M.4    Sawamura, Y.5    Diserens, A.C.6    Van Meir, E.G.7
  • 22
    • 0037779029 scopus 로고    scopus 로고
    • Probing the function of conserved residues in the serine/threonine phosphatase PP2Calpha
    • M.D. Jackson, C.C. Fjeld, and J.M. Denu Probing the function of conserved residues in the serine/threonine phosphatase PP2Calpha Biochemistry 42 2003 8513 8521
    • (2003) Biochemistry , vol.42 , pp. 8513-8521
    • Jackson, M.D.1    Fjeld, C.C.2    Denu, J.M.3
  • 25
    • 0029615509 scopus 로고
    • Protein kinase C is regulated in vivo by three functionally distinct phosphorylations
    • L.M. Keranen, E.M. Dutil, and A.C. Newton Protein kinase C is regulated in vivo by three functionally distinct phosphorylations Curr. Biol. 5 1995 1394 1403
    • (1995) Curr. Biol. , vol.5 , pp. 1394-1403
    • Keranen, L.M.1    Dutil, E.M.2    Newton, A.C.3
  • 26
    • 0034845958 scopus 로고    scopus 로고
    • PKB/Akt: A key mediator of cell proliferation, survival and insulin responses?
    • M.A. Lawlor, and D.R. Alessi PKB/Akt: a key mediator of cell proliferation, survival and insulin responses? J. Cell Sci. 114 2001 2903 2910
    • (2001) J. Cell Sci. , vol.114 , pp. 2903-2910
    • Lawlor, M.A.1    Alessi, D.R.2
  • 27
    • 0035413599 scopus 로고    scopus 로고
    • Phosphoinositide-regulated kinases and phosphoinositide phosphatases
    • N.R. Leslie, R.M. Biondi, and D.R. Alessi Phosphoinositide-regulated kinases and phosphoinositide phosphatases Chem. Rev. 101 2001 2365 2380
    • (2001) Chem. Rev. , vol.101 , pp. 2365-2380
    • Leslie, N.R.1    Biondi, R.M.2    Alessi, D.R.3
  • 28
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • T. Maehama, and J.E. Dixon The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate J. Biol. Chem. 273 1998 13375 13378
    • (1998) J. Biol. Chem. , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 29
    • 0042750799 scopus 로고    scopus 로고
    • Akt and PI 3-kinase signaling in cardiomyocyte hypertrophy and survival
    • T. Matsui, T. Nagoshi, and A. Rosenzweig Akt and PI 3-kinase signaling in cardiomyocyte hypertrophy and survival Cell Cycle 2 2003 220 223
    • (2003) Cell Cycle , vol.2 , pp. 220-223
    • Matsui, T.1    Nagoshi, T.2    Rosenzweig, A.3
  • 30
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm
    • A.C. Newton Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm Biochem. J. 370 2003 361 371
    • (2003) Biochem. J. , vol.370 , pp. 361-371
    • Newton, A.C.1
  • 31
    • 0036185848 scopus 로고    scopus 로고
    • The protein kinase B/Akt signalling pathway in human malignancy
    • K.M. Nicholson, and N.G. Anderson The protein kinase B/Akt signalling pathway in human malignancy Cell. Signal. 14 2002 381 395
    • (2002) Cell. Signal. , vol.14 , pp. 381-395
    • Nicholson, K.M.1    Anderson, N.G.2
  • 32
    • 0141639767 scopus 로고    scopus 로고
    • Autocrine signalling through erbB receptors promotes constitutive activation of protein kinase B/Akt in breast cancer cell lines
    • K.M. Nicholson, C.H. Streuli, and N.G. Anderson Autocrine signalling through erbB receptors promotes constitutive activation of protein kinase B/Akt in breast cancer cell lines Breast Cancer Res. Treat. 81 2003 117 128
    • (2003) Breast Cancer Res. Treat. , vol.81 , pp. 117-128
    • Nicholson, K.M.1    Streuli, C.H.2    Anderson, N.G.3
  • 34
    • 0032854063 scopus 로고    scopus 로고
    • SCOP, a novel gene product expressed in a circadian manner in rat suprachiasmatic nucleus
    • K. Shimizu, M. Okada, A. Takano, and K. Nagai SCOP, a novel gene product expressed in a circadian manner in rat suprachiasmatic nucleus FEBS Lett. 458 1999 363 369
    • (1999) FEBS Lett. , vol.458 , pp. 363-369
    • Shimizu, K.1    Okada, M.2    Takano, A.3    Nagai, K.4
  • 36
    • 0034708482 scopus 로고    scopus 로고
    • Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site
    • A. Toker, and A.C. Newton Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site J. Biol. Chem. 275 2000 8271 8274
    • (2000) J. Biol. Chem. , vol.275 , pp. 8271-8274
    • Toker, A.1    Newton, A.C.2
  • 37
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-Kinase AKT pathway in human cancer
    • I. Vivanco, and C.L. Sawyers The phosphatidylinositol 3-Kinase AKT pathway in human cancer Nat. Rev. Cancer 2 2002 489 501
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 38
    • 0036899518 scopus 로고    scopus 로고
    • PTEN and myotubularin phosphatases: From 3-phosphoinositide dephosphorylation to disease
    • M.J. Wishart, and J.E. Dixon PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease Trends Cell Biol. 12 2002 579 585
    • (2002) Trends Cell Biol. , vol.12 , pp. 579-585
    • Wishart, M.J.1    Dixon, J.E.2
  • 39
    • 0035895919 scopus 로고    scopus 로고
    • 3-phosphoinositide-dependent protein kinase 1, an Akt1 kinase, is involved in dephosphorylation of Thr-308 of Akt1 in Chinese hamster ovary cells
    • T. Yamada, H. Katagiri, T. Asano, K. Inukai, M. Tsuru, T. Kodama, M. Kikuchi, and Y. Oka 3-phosphoinositide-dependent protein kinase 1, an Akt1 kinase, is involved in dephosphorylation of Thr-308 of Akt1 in Chinese hamster ovary cells J. Biol. Chem. 276 2001 5339 5345
    • (2001) J. Biol. Chem. , vol.276 , pp. 5339-5345
    • Yamada, T.1    Katagiri, H.2    Asano, T.3    Inukai, K.4    Tsuru, M.5    Kodama, T.6    Kikuchi, M.7    Oka, Y.8
  • 40
    • 2542475897 scopus 로고    scopus 로고
    • Protein phosphatase-2C alpha as a positive regulator of insulin sensitivity through direct activation of phosphatidylinositol 3-kinase in 3T3-L1 adipocytes
    • T. Yoshizaki, H. Maegawa, K. Egawa, S. Ugi, Y. Nishio, T. Imamura, T. Kobayashi, S. Tamura, J.M. Olefsky, and A. Kashiwagi Protein phosphatase-2C alpha as a positive regulator of insulin sensitivity through direct activation of phosphatidylinositol 3-kinase in 3T3-L1 adipocytes J. Biol. Chem. 279 2004 22715 22726
    • (2004) J. Biol. Chem. , vol.279 , pp. 22715-22726
    • Yoshizaki, T.1    Maegawa, H.2    Egawa, K.3    Ugi, S.4    Nishio, Y.5    Imamura, T.6    Kobayashi, T.7    Tamura, S.8    Olefsky, J.M.9    Kashiwagi, A.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.