메뉴 건너뛰기




Volumn 5, Issue 10, 2014, Pages

Arrest defective 1 regulates the oxidative stress response in human cells and mice by acetylating methionine sulfoxide reductase A

Author keywords

[No Author keywords available]

Indexed keywords

ARREST DEFECTIVE 1; DNA; LYSINE; METHIONINE SULFOXIDE REDUCTASE A; OXIDIZING AGENT; REGULATOR PROTEIN; UNCLASSIFIED DRUG; METHIONINE SULFOXIDE REDUCTASE; NAA10 PROTEIN, HUMAN; NAA10 PROTEIN, MOUSE; PEPTIDE ALPHA N ACETYLTRANSFERASE A; PEPTIDE ALPHA N ACETYLTRANSFERASE E; PROTEIN BINDING;

EID: 84928016447     PISSN: None     EISSN: 20414889     Source Type: Journal    
DOI: 10.1038/cddis.2014.456     Document Type: Article
Times cited : (30)

References (44)
  • 1
    • 84892600839 scopus 로고    scopus 로고
    • Mitochondrial form and function
    • Friedman JR, Nunnari J. Mitochondrial form and function. Nature 2014; 505: 335-343.
    • (2014) Nature , vol.505 , pp. 335-343
    • Friedman, J.R.1    Nunnari, J.2
  • 3
    • 84890922670 scopus 로고    scopus 로고
    • The role of iron and reactive oxygen species in cell death
    • Dixon SJ, Stockwell BR. The role of iron and reactive oxygen species in cell death. Nat Chem Biol 2014; 10: 9-17.
    • (2014) Nat Chem Biol , vol.10 , pp. 9-17
    • Dixon, S.J.1    Stockwell, B.R.2
  • 4
    • 76749102420 scopus 로고    scopus 로고
    • Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling
    • Woo HA, Yim SH, Shin DH, Kang D, Yu DY, Rhee SG. Inactivation of peroxiredoxin I by phosphorylation allows localized H(2)O(2) accumulation for cell signaling. Cell 2010; 140: 517-528.
    • (2010) Cell , vol.140 , pp. 517-528
    • Woo, H.A.1    Yim, S.H.2    Shin, D.H.3    Kang, D.4    Yu, D.Y.5    Rhee, S.G.6
  • 5
    • 9344259718 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors
    • Kwon J, Lee SR, Yang KS, Ahn Y, Kim YJ, Stadtman ER et al. Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors. Proc Natl Acad Sci USA 2004; 101: 16419-16424.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16419-16424
    • Kwon, J.1    Lee, S.R.2    Yang, K.S.3    Ahn, Y.4    Kim, Y.J.5    Stadtman, E.R.6
  • 6
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • Sundaresan M, Yu ZX, Ferrans VJ, Irani K, Finkel T. Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science 1995; 270: 296-299.
    • (1995) Science , vol.270 , pp. 296-299
    • Sundaresan, M.1    Yu, Z.X.2    Ferrans, V.J.3    Irani, K.4    Finkel, T.5
  • 7
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • D'Autreaux B, Toledano MB. ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat Rev Mol Cell Biol 2007; 8: 813-824.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 8
    • 84874260968 scopus 로고    scopus 로고
    • A ROS rheostat for cell fate regulation
    • Maryanovich M, Gross A. A ROS rheostat for cell fate regulation. Trends Cell Biol 2013; 23: 129-134.
    • (2013) Trends Cell Biol , vol.23 , pp. 129-134
    • Maryanovich, M.1    Gross, A.2
  • 9
    • 84901052694 scopus 로고    scopus 로고
    • ROS function in redox signaling and oxidative stress
    • Schieber M, Chandel NS. ROS function in redox signaling and oxidative stress. Curr Biol 2014; 24: R453-R462.
    • (2014) Curr Biol , vol.24 , pp. R453-R462
    • Schieber, M.1    Chandel, N.S.2
  • 10
    • 0034456721 scopus 로고    scopus 로고
    • Oxidation of methionine in proteins: Roles in antioxidant defense and cellular regulation
    • Levine RL, Moskovitz J, Stadtman ER. Oxidation of methionine in proteins: roles in antioxidant defense and cellular regulation. IUBMB Life 2000; 50: 301-307.
    • (2000) IUBMB Life , vol.50 , pp. 301-307
    • Levine, R.L.1    Moskovitz, J.2    Stadtman, E.R.3
  • 11
    • 0028852816 scopus 로고
    • Oxidation of methionyl residues in proteins: Tools, targets, and reversal
    • Vogt W. Oxidation of methionyl residues in proteins: tools, targets, and reversal. Free Radic Biol Med 1995; 18: 93-105.
    • (1995) Free Radic Biol Med , vol.18 , pp. 93-105
    • Vogt, W.1
  • 12
    • 35348903730 scopus 로고    scopus 로고
    • Substrates of the methionine sulfoxide reductase system and their physiological relevance
    • Oien DB, Moskovitz J. Substrates of the methionine sulfoxide reductase system and their physiological relevance. Curr Top Dev Biol 2008; 80: 93-133.
    • (2008) Curr Top Dev Biol , vol.80 , pp. 93-133
    • Oien, D.B.1    Moskovitz, J.2
  • 13
    • 84902287070 scopus 로고
    • The physiological role of reversible methionine oxidation
    • Drazic A, Winter J. The physiological role of reversible methionine oxidation. Biochim Biophys Acta 2014; 1844: 1367-1382.
    • (1844) Biochim Biophys Acta 2014 , pp. 1367-1382
    • Drazic, A.1    Winter, J.2
  • 14
    • 84883345286 scopus 로고    scopus 로고
    • The methionine sulfoxide reduction system: Selenium utilization and methionine sulfoxide reductase enzymes and their functions
    • Kim HY. The methionine sulfoxide reduction system: selenium utilization and methionine sulfoxide reductase enzymes and their functions. Antioxid Redox Signal 2013; 19: 958-969.
    • (2013) Antioxid Redox Signal , vol.19 , pp. 958-969
    • Kim, H.Y.1
  • 15
    • 0034711184 scopus 로고    scopus 로고
    • Nalpha -terminal acetylation of eukaryotic proteins
    • Polevoda B, Sherman F. Nalpha -terminal acetylation of eukaryotic proteins. J Biol Chem 2000; 275: 36479-36482.
    • (2000) J Biol Chem , vol.275 , pp. 36479-36482
    • Polevoda, B.1    Sherman, F.2
  • 16
    • 0022407123 scopus 로고
    • The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways
    • Whiteway M, Szostak JW. The ARD1 gene of yeast functions in the switch between the mitotic cell cycle and alternative developmental pathways. Cell 1985; 43: 483-492.
    • (1985) Cell , vol.43 , pp. 483-492
    • Whiteway, M.1    Szostak, J.W.2
  • 17
    • 0141925607 scopus 로고    scopus 로고
    • An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development
    • Sugiura N, Adams SM, Corriveau RA. An evolutionarily conserved N-terminal acetyltransferase complex associated with neuronal development. J Biol Chem 2003; 278: 40113-40120.
    • (2003) J Biol Chem , vol.278 , pp. 40113-40120
    • Sugiura, N.1    Adams, S.M.2    Corriveau, R.A.3
  • 18
    • 70449379394 scopus 로고    scopus 로고
    • Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase
    • Shin DH, Chun YS, Lee KH, Shin HW, Park JW. Arrest defective-1 controls tumor cell behavior by acetylating myosin light chain kinase. PLoS One 2009; 4: e7451.
    • (2009) PLoS One , vol.4 , pp. e7451
    • Shin, D.H.1    Chun, Y.S.2    Lee, K.H.3    Shin, H.W.4    Park, J.W.5
  • 19
    • 33845293454 scopus 로고    scopus 로고
    • Human arrest defective 1 acetylates and activates beta-catenin, promoting lung cancer cell proliferation
    • Lim JH, Park JW, Chun YS. Human arrest defective 1 acetylates and activates beta-catenin, promoting lung cancer cell proliferation. Cancer Res 2006; 66: 10677-10682.
    • (2006) Cancer Res , vol.66 , pp. 10677-10682
    • Lim, J.H.1    Park, J.W.2    Chun, Y.S.3
  • 20
    • 84872613178 scopus 로고    scopus 로고
    • Protein N-terminal acetyltransferases in cancer
    • Kalvik TV, Arnesen T. Protein N-terminal acetyltransferases in cancer. Oncogene 2013; 32: 269-276.
    • (2013) Oncogene , vol.32 , pp. 269-276
    • Kalvik, T.V.1    Arnesen, T.2
  • 21
    • 75149114580 scopus 로고    scopus 로고
    • Protein carbonyl and the methionine sulfoxide reductase system
    • Moskovitz J, Oien DB. Protein carbonyl and the methionine sulfoxide reductase system. Antioxid Redox Signal 2010; 12: 405-415.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 405-415
    • Moskovitz, J.1    Oien, D.B.2
  • 22
    • 17844403545 scopus 로고    scopus 로고
    • Role of oxidative carbonylation in protein quality control and senescence
    • Nystrom T. Role of oxidative carbonylation in protein quality control and senescence. EMBO J 2005; 24: 1311-1317.
    • (2005) EMBO J , vol.24 , pp. 1311-1317
    • Nystrom, T.1
  • 23
    • 0343280013 scopus 로고    scopus 로고
    • A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage
    • Paull TT, Rogakou EP, Yamazaki V, Kirchgessner CU, Gellert M, Bonner WM. A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage. Curr Biol 2000; 10: 886-895.
    • (2000) Curr Biol , vol.10 , pp. 886-895
    • Paull, T.T.1    Rogakou, E.P.2    Yamazaki, V.3    Kirchgessner, C.U.4    Gellert, M.5    Bonner, W.M.6
  • 24
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakou EP, Pilch DR, Orr AH, Ivanova VS, Bonner WM. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J Biol Chem 1998; 273: 5858-5868.
    • (1998) J Biol Chem , vol.273 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.S.4    Bonner, W.M.5
  • 25
    • 77956218104 scopus 로고    scopus 로고
    • Phenethyl isothiocyanate inhibits oxidative phosphorylation to trigger reactive oxygen species-mediated death of human prostate cancer cells
    • Xiao D, Powolny AA, Moura MB, Kelley EE, Bommareddy A, Kim SH et al. Phenethyl isothiocyanate inhibits oxidative phosphorylation to trigger reactive oxygen species-mediated death of human prostate cancer cells. J Biol Chem 2010; 285: 26558-26569.
    • (2010) J Biol Chem , vol.285 , pp. 26558-26569
    • Xiao, D.1    Powolny, A.A.2    Moura, M.B.3    Kelley, E.E.4    Bommareddy, A.5    Kim, S.H.6
  • 26
    • 0033389391 scopus 로고    scopus 로고
    • Mini-review: Discovery and development of platinum complexes designed to circumvent cisplatin resistance
    • Kelland LR, Sharp SY, O'Neill CF, Raynaud FI, Beale PJ, Judson IR. Mini-review: discovery and development of platinum complexes designed to circumvent cisplatin resistance. J Inorg Biochem 1999; 77: 111-115.
    • (1999) J Inorg Biochem , vol.77 , pp. 111-115
    • Kelland, L.R.1    Sharp, S.Y.2    O'Neill, C.F.3    Raynaud, F.I.4    Beale, P.J.5    Judson, I.R.6
  • 27
    • 84862677510 scopus 로고    scopus 로고
    • Focus on molecules: Methionine sulfoxide reductase A
    • Kantorow M, Lee W, Chauss D. Focus on molecules: methionine sulfoxide reductase A. Exp Eye Res 2012; 100: 110-111.
    • (2012) Exp Eye Res , vol.100 , pp. 110-111
    • Kantorow, M.1    Lee, W.2    Chauss, D.3
  • 28
    • 35748932403 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: Selenoprotein forms and roles in antioxidant protein repair in mammals
    • Kim HY, Gladyshev VN. Methionine sulfoxide reductases: selenoprotein forms and roles in antioxidant protein repair in mammals. Biochem J 2007; 407: 321-329.
    • (2007) Biochem J , vol.407 , pp. 321-329
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 29
    • 84886382595 scopus 로고    scopus 로고
    • A specific and rapid colorimetric method to monitor the activity of methionine sulfoxide reductase A
    • Wu PF, Zhang Z, Guan XL, Li YL, Zeng JH, Zhang JJ et al. A specific and rapid colorimetric method to monitor the activity of methionine sulfoxide reductase A. Enzyme Microb Technol 2013; 53: 391-397.
    • (2013) Enzyme Microb Technol , vol.53 , pp. 391-397
    • Wu, P.F.1    Zhang, Z.2    Guan, X.L.3    Li, Y.L.4    Zeng, J.H.5    Zhang, J.J.6
  • 30
    • 0142151375 scopus 로고    scopus 로고
    • Oxidation of methionine residues of proteins: Biological consequences
    • Stadtman ER, Moskovitz J, Levine RL. Oxidation of methionine residues of proteins: biological consequences. Antioxid Redox Signal 2003; 5: 577-582.
    • (2003) Antioxid Redox Signal , vol.5 , pp. 577-582
    • Stadtman, E.R.1    Moskovitz, J.2    Levine, R.L.3
  • 34
    • 3042834124 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress
    • Kantorow M, Hawse JR, Cowell TL, Benhamed S, Pizarro GO, Reddy VN et al. Methionine sulfoxide reductase A is important for lens cell viability and resistance to oxidative stress. Proc Natl Acad Sci USA 2004; 101: 9654-9659.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9654-9659
    • Kantorow, M.1    Hawse, J.R.2    Cowell, T.L.3    Benhamed, S.4    Pizarro, G.O.5    Reddy, V.N.6
  • 35
    • 70349693474 scopus 로고    scopus 로고
    • Lack of methionine sulfoxide reductase A in mice increases sensitivity to oxidative stress but does not diminish life span
    • Salmon AB, Perez VI, Bokov A, Jernigan A, Kim G, Zhao H et al. Lack of methionine sulfoxide reductase A in mice increases sensitivity to oxidative stress but does not diminish life span. FASEB J 2009; 23: 3601-3608.
    • (2009) FASEB J , vol.23 , pp. 3601-3608
    • Salmon, A.B.1    Perez, V.I.2    Bokov, A.3    Jernigan A.Kim, G.4    Zhao, H.5
  • 36
    • 42949085382 scopus 로고    scopus 로고
    • A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation
    • Erickson JR, Joiner ML, Guan X, Kutschke W, Yang J, Oddis CV et al. A dynamic pathway for calcium-independent activation of CaMKII by methionine oxidation. Cell 2008; 133: 462-474.
    • (2008) Cell , vol.133 , pp. 462-474
    • Erickson, J.R.1    Joiner, M.L.2    Guan, X.3    Kutschke, W.4    Yang, J.5    Oddis, C.V.6
  • 37
    • 59649127414 scopus 로고    scopus 로고
    • Methionine in proteins defends against oxidative stress
    • Luo S, Levine RL. Methionine in proteins defends against oxidative stress. FASEB j 2009; 23: 464-472.
    • (2009) FASEB j , vol.23 , pp. 464-472
    • Luo, S.1    Levine, R.L.2
  • 39
    • 84876929380 scopus 로고    scopus 로고
    • Protective role of methionine sulfoxide reductase A against ischemia/reperfusion injury in mouse kidney and its involvement in the regulation of trans-sulfuration pathway
    • Kim JI, Choi SH, Jung KJ, Lee E, Kim HY, Park KM. Protective role of methionine sulfoxide reductase A against ischemia/reperfusion injury in mouse kidney and its involvement in the regulation of trans-sulfuration pathway. Antioxid Redox Signal 2013; 18: 2241-2250.
    • (2013) Antioxid Redox Signal , vol.18 , pp. 2241-2250
    • Kim, J.I.1    Choi, S.H.2    Jung, K.J.3    Lee, E.4    Kim, H.Y.5    Park, K.M.6
  • 40
    • 0029294613 scopus 로고
    • In situ detection of fragmented DNA (TUNEL assay) fails to discriminate among apoptosis, necrosis, and autolytic cell death: A cautionary note
    • Grasl-Kraupp B, Ruttkay-Nedecky B, Koudelka H, Bukowska K, Bursch W, Schulte-Hermann R. In situ detection of fragmented DNA (TUNEL assay) fails to discriminate among apoptosis, necrosis, and autolytic cell death: a cautionary note. Hepatology 1995; 21: 1465-1468.
    • (1995) Hepatology , vol.21 , pp. 1465-1468
    • Grasl-Kraupp, B.1    Ruttkay-Nedecky, B.2    Koudelka, H.3    Bukowska, K.4    Bursch, W.5    Schulte-Hermann, R.6
  • 41
    • 18744375998 scopus 로고    scopus 로고
    • Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation
    • Jeong JW, Bae MK, Ahn MY, Kim SH, Sohn TK, Bae MH et al. Regulation and destabilization of HIF-1alpha by ARD1-mediated acetylation. Cell 2002; 111: 709-720.
    • (2002) Cell , vol.111 , pp. 709-720
    • Jeong, J.W.1    Bae, M.K.2    Ahn, M.Y.3    Kim, S.H.4    Sohn, T.K.5    Bae, M.H.6
  • 42
    • 27744450043 scopus 로고    scopus 로고
    • Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha
    • Arnesen T, Kong X, Evjenth R, Gromyko D, Varhaug JE, Lin Z et al. Interaction between HIF-1 alpha (ODD) and hARD1 does not induce acetylation and destabilization of HIF-1 alpha. FEBS Lett 2005; 579: 6428-6432.
    • (2005) FEBS Lett , vol.579 , pp. 6428-6432
    • Arnesen, T.1    Kong, X.2    Evjenth, R.3    Gromyko, D.4    Varhaug, J.E.5    Lin, Z.6
  • 43
    • 69849097192 scopus 로고    scopus 로고
    • Mitochondrial generation of free radicals and hypoxic signaling
    • Poyton RO, Ball KA, Castello PR. Mitochondrial generation of free radicals and hypoxic signaling. Trends Endocrinol Metab 2009; 20: 332-340.
    • (2009) Trends Endocrinol Metab , vol.20 , pp. 332-340
    • Poyton, R.O.1    Ball, K.A.2    Castello, P.R.3
  • 44
    • 77949943221 scopus 로고    scopus 로고
    • Roles of arrest-defective protein 1 (225) and hypoxia-inducible factor 1alpha in tumor growth and metastasis
    • Lee MN, Lee SN, Kim SH, Kim B, Jung BK, Seo JH et al. Roles of arrest-defective protein 1 (225) and hypoxia-inducible factor 1alpha in tumor growth and metastasis. J Natl Cancer Inst 2010; 102: 426-442.
    • (2010) J Natl Cancer Inst , vol.102 , pp. 426-442
    • Lee, M.N.1    Lee, S.N.2    Kim, S.H.3    Kim, B.4    Jung, B.K.5    Seo, J.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.