메뉴 건너뛰기




Volumn 9, Issue 1, 2014, Pages

PR65A phosphorylation regulates PP2A complex signaling

Author keywords

[No Author keywords available]

Indexed keywords

ANNEXIN A; BIOLOGICAL MARKER; CHAPERONIN 60; ELONGATION FACTOR 1ALPHA; ELONGATION FACTOR 2; PHOSPHOPROTEIN PHOSPHATASE 2A; PR65A PROTEIN; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84897410573     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0085000     Document Type: Article
Times cited : (10)

References (36)
  • 1
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • DOI 10.1042/0264-6021:3530417
    • Janssens V, Goris J (2001) Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem J 353: 417-439. (Pubitemid 32158309)
    • (2001) Biochemical Journal , vol.353 , Issue.3 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 2
    • 70350340056 scopus 로고    scopus 로고
    • Serine/threonine phosphatases: Mechanism through structure
    • Shi Y (2009) Serine/threonine phosphatases: mechanism through structure. Cell 139:468-484.
    • (2009) Cell , vol.139 , pp. 468-484
    • Shi, Y.1
  • 3
    • 43149103684 scopus 로고    scopus 로고
    • PP2A regulates the pro-apoptotic activity of FOXO1
    • Yan L, Lavin VA, Moser LR, Cui Q, Kanies C, et al. (2008) PP2A regulates the pro-apoptotic activity of FOXO1. J Biol Chem 283: 7411-7420.
    • (2008) J Biol Chem , vol.283 , pp. 7411-7420
    • Yan, L.1    Lavin, V.A.2    Moser, L.R.3    Cui, Q.4    Kanies, C.5
  • 4
    • 34447106751 scopus 로고    scopus 로고
    • PP2A: Unveiling a reluctant tumor suppressor
    • Mumby M (2007) PP2A: unveiling a reluctant tumor suppressor. Cell 130: 21-24.
    • (2007) Cell , vol.130 , pp. 21-24
    • Mumby, M.1
  • 5
    • 79952611078 scopus 로고    scopus 로고
    • Impaired beta-adrenergic responsiveness accentuates dysfunctional excitation-contraction coupling in an ovine model of tachypacing-induced heart failure
    • Briston SJ, Caldwell JL, Horn MA, Clarke JD, Richards MA, et al. (2011) Impaired beta-adrenergic responsiveness accentuates dysfunctional excitation-contraction coupling in an ovine model of tachypacing-induced heart failure. J Physiol 589: 1367-1382.
    • (2011) J Physiol , vol.589 , pp. 1367-1382
    • Briston, S.J.1    Caldwell, J.L.2    Horn, M.A.3    Clarke, J.D.4    Richards, M.A.5
  • 6
    • 11844254718 scopus 로고    scopus 로고
    • Connexin 43 downregulation and dephosphorylation in nonischemic heart failure is associated with enhanced colocalized protein phosphatase type 2A
    • DOI 10.1161/01.RES.0000152325.07495.5a
    • Ai X, Pogwizd SM (2005) Connexin 43 downregulation and dephosphorylation in nonischemic heart failure is associated with enhanced colocalized protein phosphatase type 2A. Circ Res 96: 54-63. (Pubitemid 40095754)
    • (2005) Circulation Research , vol.96 , Issue.1 , pp. 54-63
    • Ai, X.1    Pogwizd, S.M.2
  • 7
    • 61849127277 scopus 로고    scopus 로고
    • Peroxynitrite Increases Protein Phosphatase Activity and Promotes the Interaction of Phospholamban with Protein Phosphatase 2a in the Myocardium
    • Kohr MJ, Davis JP, Ziolo MT (2009) Peroxynitrite Increases Protein Phosphatase Activity and Promotes the Interaction of Phospholamban with Protein Phosphatase 2a in the Myocardium. Nitric Oxide 20: 217-221.
    • (2009) Nitric Oxide , vol.20 , pp. 217-221
    • Kohr, M.J.1    Davis, J.P.2    Ziolo, M.T.3
  • 8
    • 0025360568 scopus 로고
    • 2+ uptake in sarcoplasmic reticulum from normal and failing hearts
    • Movsesian MA, Colyer J, Wang JH, Krall J (1990) Phospholamban-mediated stimulation of Ca2+ uptake in sarcoplasmic reticulum from normal and failing hearts. J Clin Invest 85: 1698-1702. (Pubitemid 20176470)
    • (1990) Journal of Clinical Investigation , vol.85 , Issue.5 , pp. 1698-1702
    • Movsesian, M.A.1    Colyer, J.2    Wang, J.H.3    Krall, J.4
  • 9
    • 52049115619 scopus 로고    scopus 로고
    • Phospholamban phosphorylation by CaMKII under pathophysiological conditions
    • Vittone L, Mundina-Weilenmann C, Mattiazzi A (2008) Phospholamban phosphorylation by CaMKII under pathophysiological conditions. Front Biosci 13: 5988-6005.
    • (2008) Front Biosci , vol.13 , pp. 5988-6005
    • Vittone, L.1    Mundina-Weilenmann, C.2    Mattiazzi, A.3
  • 10
    • 0029120983 scopus 로고
    • Response of failing canine and human heart cells to beta 2-adrenergic stimulation
    • Altschuld RA, Starling RC, Hamlin RL, Billman GE, Hensley J, et al. (1995) Response of failing canine and human heart cells to beta 2-adrenergic stimulation. Circulation 92: 1612-1618.
    • (1995) Circulation , vol.92 , pp. 1612-1618
    • Altschuld, R.A.1    Starling, R.C.2    Hamlin, R.L.3    Billman, G.E.4    Hensley, J.5
  • 11
    • 1042279545 scopus 로고    scopus 로고
    • 21-Activated Kinase-1 (Pak1) in Cardiac Myocytes
    • DOI 10.1161/01.RES.0000111522.02730.56
    • Ke Y, Wang L, Pyle WG, de Tombe PP, Solaro RJ (2004) Intracellular localization and functional effects of P21-activated kinase-1 (Pak1) in cardiac myocytes. Circ Res 94: 194-200. (Pubitemid 38197451)
    • (2004) Circulation Research , vol.94 , Issue.2 , pp. 194-200
    • Ke, Y.1    Wang, L.2    Pyle, W.G.3    De Tombe, P.P.4    Solaro, R.J.5
  • 13
    • 0037144667 scopus 로고    scopus 로고
    • p21-activated kinase increases the calcium sensitivity of rat triton-skinned cardiac muscle fiber bundles via a mechanism potentially involving novel phosphorylation of troponin I
    • Buscemi N, Foster DB, Neverova I, Van Eyk JE (2002) p21-activated kinase increases the calcium sensitivity of rat triton-skinned cardiac muscle fiber bundles via a mechanism potentially involving novel phosphorylation of troponin I. Circ Res 91: 509-516.
    • (2002) Circ Res , vol.91 , pp. 509-516
    • Buscemi, N.1    Foster, D.B.2    Neverova, I.3    Van Eyk, J.E.4
  • 14
    • 79958111532 scopus 로고    scopus 로고
    • PP2A in the regulation of cell motility and invasion
    • Basu S (2011) PP2A in the regulation of cell motility and invasion. Curr Protein Pept Sci 12: 3-11.
    • (2011) Curr Protein Pept Sci , vol.12 , pp. 3-11
    • Basu, S.1
  • 15
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • DOI 10.1042/0264-6021:3530417
    • Janssens V, Goris J (2001) Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem J 353: 417-439. (Pubitemid 32158309)
    • (2001) Biochemical Journal , vol.353 , Issue.3 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 17
    • 33846118688 scopus 로고    scopus 로고
    • Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
    • DOI 10.1038/nature05351, PII NATURE05351
    • Cho US, Xu W (2007) Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme. Nature 445: 53-57. (Pubitemid 46067298)
    • (2007) Nature , vol.445 , Issue.7123 , pp. 53-57
    • Cho, U.S.1    Xu, W.2
  • 18
    • 52049100425 scopus 로고    scopus 로고
    • Structure of a protein phosphatase 2A holoenzyme: Insights into B55-mediated Tau dephosphorylation
    • Xu Y, Chen Y, Zhang P, Jeffrey PD, Shi Y (2008) Structure of a protein phosphatase 2A holoenzyme: insights into B55-mediated Tau dephosphorylation. Mol Cell 31: 873-885.
    • (2008) Mol Cell , vol.31 , pp. 873-885
    • Xu, Y.1    Chen, Y.2    Zhang, P.3    Jeffrey, P.D.4    Shi, Y.5
  • 19
    • 0028082299 scopus 로고
    • Molecular model of the A subunit of protein phosphatase 2A: Interaction with other subunits and tumor antigens
    • Ruediger R, Hentz M, Fait J, Mumby M, Walter G (1994) Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens. J Virol 68: 123-129.
    • (1994) J Virol , vol.68 , pp. 123-129
    • Ruediger, R.1    Hentz, M.2    Fait, J.3    Mumby, M.4    Walter, G.5
  • 20
    • 0026661827 scopus 로고
    • Identification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of simian virus 40 and polyomavirus
    • Ruediger R, Roeckel D, Fait J, Bergqvist A, Magnusson G, et al. (1992) Identification of binding sites on the regulatory A subunit of protein phosphatase 2A for the catalytic C subunit and for tumor antigens of simian virus 40 and polyomavirus. Mol Cell Biol 12: 4872-4882.
    • (1992) Mol Cell Biol , vol.12 , pp. 4872-4882
    • Ruediger, R.1    Roeckel, D.2    Fait, J.3    Bergqvist, A.4    Magnusson, G.5
  • 21
    • 84872287681 scopus 로고    scopus 로고
    • Molecular mechanisms underlying cardiac protein phosphatase 2A regulation in heart
    • DeGrande ST, Little SC, Nixon DJ, Wright P, Snyder J, et al. (2013) Molecular mechanisms underlying cardiac protein phosphatase 2A regulation in heart. J Biol Chem 288: 1032-1046.
    • (2013) J Biol Chem , vol.288 , pp. 1032-1046
    • DeGrande, S.T.1    Little, S.C.2    Nixon, D.J.3    Wright, P.4    Snyder, J.5
  • 24
    • 84879888186 scopus 로고    scopus 로고
    • Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation
    • Wlodarchak N, Guo F, Satyshur KA, Jiang L, Jeffrey PD, et al. (2013) Structure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylation. Cell Res 23: 931-946.
    • (2013) Cell Res , vol.23 , pp. 931-946
    • Wlodarchak, N.1    Guo, F.2    Satyshur, K.A.3    Jiang, L.4    Jeffrey, P.D.5
  • 26
    • 0035799352 scopus 로고    scopus 로고
    • Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation
    • Lin KM, Lin B, Lian IY, Mestril R, Scheffler IE, et al. (2001) Combined and individual mitochondrial HSP60 and HSP10 expression in cardiac myocytes protects mitochondrial function and prevents apoptotic cell deaths induced by simulated ischemia-reoxygenation. Circulation 103: 1787-1792. (Pubitemid 32291417)
    • (2001) Circulation , vol.103 , Issue.13 , pp. 1787-1792
    • Lin, K.M.1    Lin, B.2    Lian, I.Y.3    Mestril, R.4    Scheffler, I.E.5    Dillmann, W.H.6
  • 27
    • 51749114010 scopus 로고    scopus 로고
    • Relation of serum heat shock protein 60 level to severity and prognosis in chronic heart failure secondary to ischemic or idiopathic dilated cardiomyopathy
    • Niizeki T, Takeishi Y, Watanabe T, Nitobe J, Miyashita T, et al. (2008) Relation of serum heat shock protein 60 level to severity and prognosis in chronic heart failure secondary to ischemic or idiopathic dilated cardiomyopathy. Am J Cardiol 102: 606-610.
    • (2008) Am J Cardiol , vol.102 , pp. 606-610
    • Niizeki, T.1    Takeishi, Y.2    Watanabe, T.3    Nitobe, J.4    Miyashita, T.5
  • 28
    • 0032168039 scopus 로고    scopus 로고
    • Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane
    • DOI 10.1073/pnas.95.18.10425
    • Khan IU, Wallin R, Gupta RS, Kammer GM (1998) Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane. Proc Natl Acad Sci U S A 95: 10425-10430. (Pubitemid 28413083)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.18 , pp. 10425-10430
    • Khan, I.U.1    Wallin, R.2    Gupta, R.S.3    Kammer, G.M.4
  • 29
    • 79956298543 scopus 로고    scopus 로고
    • A small molecule AMPK activator protects the heart against ischemia-reperfusion injury
    • Kim AS, Miller EJ, Wright TM, Li J, Qi D, et al. (2011) A small molecule AMPK activator protects the heart against ischemia-reperfusion injury. J Mol Cell Cardiol 51: 24-32.
    • (2011) J Mol Cell Cardiol , vol.51 , pp. 24-32
    • Kim, A.S.1    Miller, E.J.2    Wright, T.M.3    Li, J.4    Qi, D.5
  • 30
    • 84872857473 scopus 로고    scopus 로고
    • Reperfusion-Induced Myocardial Dysfunction is Prevented by Endogenous Annexin-A1 And Its N-terminal Derived Peptide Ac-ANX-A1 (2-26)
    • Qin C, Buxton KD, Pepe S, Cao AH, Venardos K, et al. (2012) Reperfusion-Induced Myocardial Dysfunction is Prevented by Endogenous Annexin-A1 And Its N-terminal Derived Peptide Ac-ANX-A1 (2-26). Br J Pharmacol.
    • (2012) Br J Pharmacol
    • Qin, C.1    Buxton, K.D.2    Pepe, S.3    Cao, A.H.4    Venardos, K.5
  • 31
    • 70350125759 scopus 로고    scopus 로고
    • Exploiting the Annexin A1 pathway for the development of novel anti-inflammatory therapeutics
    • Perretti M, Dalli J (2009) Exploiting the Annexin A1 pathway for the development of novel anti-inflammatory therapeutics. Br J Pharmacol 158: 936-946.
    • (2009) Br J Pharmacol , vol.158 , pp. 936-946
    • Perretti, M.1    Dalli, J.2
  • 32
    • 12244267108 scopus 로고    scopus 로고
    • Cardioprotective actions of an N-terminal fragment of annexin-1 in rat myocardium in vitro
    • DOI 10.1016/S0014-2999(03)01314-1
    • Ritchie RH, Sun X, Bilszta JL, Gulluyan LM, Dusting GJ (2003) Cardioprotective actions of an N-terminal fragment of annexin-1 in rat myocardium in vitro. Eur J Pharmacol 461: 171-179. (Pubitemid 36174035)
    • (2003) European Journal of Pharmacology , vol.461 , Issue.2-3 , pp. 171-179
    • Ritchie, R.H.1    Sun, X.2    Bilszta, J.L.3    Gulluyan, L.M.4    Dusting, G.J.5
  • 33
    • 79952927802 scopus 로고    scopus 로고
    • Phosphorylation of annexin A1 by TRPM7 kinase: A switch regulating the induction of an alpha-helix
    • Dorovkov MV, Kostyukova AS, Ryazanov AG (2011) Phosphorylation of annexin A1 by TRPM7 kinase: a switch regulating the induction of an alpha-helix. Biochemistry 50: 2187-2193.
    • (2011) Biochemistry , vol.50 , pp. 2187-2193
    • Dorovkov, M.V.1    Kostyukova, A.S.2    Ryazanov, A.G.3
  • 34
    • 84866095385 scopus 로고    scopus 로고
    • Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry
    • Herzog F, Kahraman A, Boehringer D, Mak R, Bracher A, et al. (2012) Structural probing of a protein phosphatase 2A network by chemical cross-linking and mass spectrometry. Science 337: 1348-1352.
    • (2012) Science , vol.337 , pp. 1348-1352
    • Herzog, F.1    Kahraman, A.2    Boehringer, D.3    Mak, R.4    Bracher, A.5
  • 35
    • 79951851366 scopus 로고    scopus 로고
    • Regulation of Protein Kinase C function by phosphorylation on conserved and non-conserved sites
    • Freeley M, Kelleher D, Long A (2011) Regulation of Protein Kinase C function by phosphorylation on conserved and non-conserved sites. Cell Signal 23: 753-762.
    • (2011) Cell Signal , vol.23 , pp. 753-762
    • Freeley, M.1    Kelleher, D.2    Long, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.