메뉴 건너뛰기




Volumn 21, Issue 3, 2006, Pages 349-357

Regulation of SUMOylation by reversible oxidation of SUMO conjugating enzymes

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; REACTIVE OXYGEN METABOLITE; SUMO PROTEIN; TRANSCRIPTION FACTOR;

EID: 31544432283     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.12.019     Document Type: Article
Times cited : (322)

References (49)
  • 2
    • 0346422441 scopus 로고    scopus 로고
    • Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1
    • D. Bailey, and P. O'Hare Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1 J. Biol. Chem. 279 2004 692 703
    • (2004) J. Biol. Chem. , vol.279 , pp. 692-703
    • Bailey, D.1    O'Hare, P.2
  • 3
    • 9944235916 scopus 로고    scopus 로고
    • The role of cysteine residues as redox-sensitive regulatory switches
    • D. Barford The role of cysteine residues as redox-sensitive regulatory switches Curr. Opin. Struct. Biol. 14 2004 679 686
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 679-686
    • Barford, D.1
  • 4
    • 0035984912 scopus 로고    scopus 로고
    • ROS, stress-activated kinases and stress signaling in cancer
    • M. Benhar, D. Engelberg, and A. Levitzki ROS, stress-activated kinases and stress signaling in cancer EMBO Rep. 3 2002 420 425
    • (2002) EMBO Rep. , vol.3 , pp. 420-425
    • Benhar, M.1    Engelberg, D.2    Levitzki, A.3
  • 8
    • 8744276616 scopus 로고    scopus 로고
    • Amyloid beta-peptide(1-42) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain
    • D.A. Butterfield, and D. Boyd-Kimball Amyloid beta-peptide(1-42) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain Brain Pathol. 14 2004 426 432
    • (2004) Brain Pathol. , vol.14 , pp. 426-432
    • Butterfield, D.A.1    Boyd-Kimball, D.2
  • 9
    • 0037376674 scopus 로고    scopus 로고
    • Oxidant signals and oxidative stress
    • T. Finkel Oxidant signals and oxidative stress Curr. Opin. Cell Biol. 15 2003 247 254
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 247-254
    • Finkel, T.1
  • 10
    • 0037382641 scopus 로고    scopus 로고
    • Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity
    • G. Gill Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity Curr. Opin. Genet. Dev. 13 2003 108 113
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 108-113
    • Gill, G.1
  • 11
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms?
    • G. Gill SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? Genes Dev. 18 2004 2046 2059
    • (2004) Genes Dev. , vol.18 , pp. 2046-2059
    • Gill, G.1
  • 12
    • 0032998598 scopus 로고    scopus 로고
    • Intracellular oxidation/reduction status in the regulation of transcription factors NF-kappaB and AP-1
    • D. Gius, A. Botero, S. Shah, and H.A. Curry Intracellular oxidation/reduction status in the regulation of transcription factors NF-kappaB and AP-1 Toxicol. Lett. 106 1999 93 106
    • (1999) Toxicol. Lett. , vol.106 , pp. 93-106
    • Gius, D.1    Botero, A.2    Shah, S.3    Curry, H.A.4
  • 13
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, and A. Ciechanover The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction Physiol. Rev. 82 2002 373 428
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 14
    • 0021684935 scopus 로고
    • Priming of neutrophils for enhanced release of oxygen metabolites by bacterial lipopolysaccharide. Evidence for increased activity of the superoxide-producing enzyme
    • L.A. Guthrie, L.C. McPhail, P.M. Henson, and R.B. Johnston Jr. Priming of neutrophils for enhanced release of oxygen metabolites by bacterial lipopolysaccharide. Evidence for increased activity of the superoxide-producing enzyme J. Exp. Med. 160 1984 1656 1671
    • (1984) J. Exp. Med. , vol.160 , pp. 1656-1671
    • Guthrie, L.A.1    McPhail, L.C.2    Henson, P.M.3    Johnston Jr., R.B.4
  • 15
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • R.T. Hay SUMO: a history of modification Mol. Cell 18 2005 1 12
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 16
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • A. Hershko, and A. Ciechanover The ubiquitin system for protein degradation Annu. Rev. Biochem. 61 1992 761 807
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 17
    • 0141442586 scopus 로고    scopus 로고
    • Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins
    • L. Hicke, and R. Dunn Regulation of membrane protein transport by ubiquitin and ubiquitin-binding proteins Annu. Rev. Cell Dev. Biol. 19 2003 141 172
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 141-172
    • Hicke, L.1    Dunn, R.2
  • 18
    • 0036395928 scopus 로고    scopus 로고
    • Macrophage signaling and respiratory burst
    • K.E. Iles, and H.J. Forman Macrophage signaling and respiratory burst Immunol. Res. 26 2002 95 105
    • (2002) Immunol. Res. , vol.26 , pp. 95-105
    • Iles, K.E.1    Forman, H.J.2
  • 19
    • 0034256031 scopus 로고    scopus 로고
    • Ubiquitin and its kin: How close are the family ties?
    • S. Jentsch, and G. Pyrowolakis Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 10 2000 335 342
    • (2000) Trends Cell Biol. , vol.10 , pp. 335-342
    • Jentsch, S.1    Pyrowolakis, G.2
  • 20
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • E.S. Johnson Protein modification by SUMO Annu. Rev. Biochem. 73 2004 355 382
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 21
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • H. Kamata, S. Honda, S. Maeda, L. Chang, H. Hirata, and M. Karin Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases Cell 120 2005 649 661
    • (2005) Cell , vol.120 , pp. 649-661
    • Kamata, H.1    Honda, S.2    Maeda, S.3    Chang, L.4    Hirata, H.5    Karin, M.6
  • 23
    • 9344259718 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors
    • J. Kwon, S.R. Lee, K.S. Yang, Y. Ahn, Y.J. Kim, E.R. Stadtman, and S.G. Rhee Reversible oxidation and inactivation of the tumor suppressor PTEN in cells stimulated with peptide growth factors Proc. Natl. Acad. Sci. USA 101 2004 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    Rhee, S.G.7
  • 24
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • J.D. Lambeth NOX enzymes and the biology of reactive oxygen Nat. Rev. Immunol. 4 2004 181 189
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 25
    • 0032512922 scopus 로고    scopus 로고
    • Modification of Ran GTPase-activating protein by the Small Ubiquitin-related Modifier SUMO-1 requires Ubc9, an E2-type Ubiquitin- conjugating enzyme homologue
    • G.W. Lee, F. Melchior, M.J. Matunis, R. Mahajan, Q. Tian, and P. Anderson Modification of Ran GTPase-activating protein by the Small Ubiquitin-related Modifier SUMO-1 requires Ubc9, an E2-type Ubiquitin-conjugating enzyme homologue J. Biol. Chem. 273 1998 6503 6507
    • (1998) J. Biol. Chem. , vol.273 , pp. 6503-6507
    • Lee, G.W.1    Melchior, F.2    Matunis, M.J.3    Mahajan, R.4    Tian, Q.5    Anderson, P.6
  • 27
    • 14844291338 scopus 로고    scopus 로고
    • Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1
    • L.M. Lois, and C.D. Lima Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1 EMBO J. 24 2005 439 451
    • (2005) EMBO J. , vol.24 , pp. 439-451
    • Lois, L.M.1    Lima, C.D.2
  • 28
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • R. Mahajan, C. Delphin, T. Guan, L. Gerace, and F. Melchior A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2 Cell 88 1997 97 107
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 30
    • 13644268060 scopus 로고    scopus 로고
    • Cell biology. SUMO wrestles its way to prominence in the cell
    • J. Marx Cell biology. SUMO wrestles its way to prominence in the cell Science 307 2005 836 839
    • (2005) Science , vol.307 , pp. 836-839
    • Marx, J.1
  • 33
    • 0036184190 scopus 로고    scopus 로고
    • Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo
    • T.C. Meng, T. Fukada, and N.K. Tonks Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo Mol. Cell 9 2002 387 399
    • (2002) Mol. Cell , vol.9 , pp. 387-399
    • Meng, T.C.1    Fukada, T.2    Tonks, N.K.3
  • 35
    • 0026062962 scopus 로고
    • Assembly of the neutrophil respiratory burst oxidase. Protein kinase C promotes cytoskeletal and membrane association of cytosolic oxidase components
    • W.M. Nauseef, B.D. Volpp, S. McCormick, K.G. Leidal, and R.A. Clark Assembly of the neutrophil respiratory burst oxidase. Protein kinase C promotes cytoskeletal and membrane association of cytosolic oxidase components J. Biol. Chem. 266 1991 5911 5917
    • (1991) J. Biol. Chem. , vol.266 , pp. 5911-5917
    • Nauseef, W.M.1    Volpp, B.D.2    McCormick, S.3    Leidal, K.G.4    Clark, R.A.5
  • 36
    • 0036174453 scopus 로고    scopus 로고
    • Oxidative damage and cancer
    • T.D. Oberley Oxidative damage and cancer Am. J. Pathol. 160 2002 403 408
    • (2002) Am. J. Pathol. , vol.160 , pp. 403-408
    • Oberley, T.D.1
  • 37
    • 0035823543 scopus 로고    scopus 로고
    • Protein tyrosine nitration in cytokine-activated murine macrophages. Involvement of a peroxidase/nitrite pathway rather than peroxynitrite
    • S. Pfeiffer, A. Lass, K. Schmidt, and B. Mayer Protein tyrosine nitration in cytokine-activated murine macrophages. Involvement of a peroxidase/nitrite pathway rather than peroxynitrite J. Biol. Chem. 276 2001 34051 34058
    • (2001) J. Biol. Chem. , vol.276 , pp. 34051-34058
    • Pfeiffer, S.1    Lass, A.2    Schmidt, K.3    Mayer, B.4
  • 38
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • A. Pichler, A. Gast, J.S. Seeler, A. Dejean, and F. Melchior The nucleoporin RanBP2 has SUMO1 E3 ligase activity Cell 108 2002 109 120
    • (2002) Cell , vol.108 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 39
    • 0842303313 scopus 로고    scopus 로고
    • Back to the future with ubiquitin
    • C.M. Pickart Back to the future with ubiquitin Cell 116 2004 181 190
    • (2004) Cell , vol.116 , pp. 181-190
    • Pickart, C.M.1
  • 40
    • 17044428567 scopus 로고    scopus 로고
    • Sumoylation silences the plasma membrane leak K+ channel K2P1
    • S. Rajan, L.D. Plant, M.L. Rabin, M.H. Butler, and S.A. Goldstein Sumoylation silences the plasma membrane leak K+ channel K2P1 Cell 121 2005 37 47
    • (2005) Cell , vol.121 , pp. 37-47
    • Rajan, S.1    Plant, L.D.2    Rabin, M.L.3    Butler, M.H.4    Goldstein, S.A.5
  • 41
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • S.G. Rhee, S.W. Kang, W. Jeong, T.S. Chang, K.S. Yang, and H.A. Woo Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins Curr. Opin. Cell Biol. 17 2005 183 189
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 183-189
    • Rhee, S.G.1    Kang, S.W.2    Jeong, W.3    Chang, T.S.4    Yang, K.S.5    Woo, H.A.6
  • 42
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • H. Saitoh, and J. Hinchey Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3 J. Biol. Chem. 275 2000 6252 6258
    • (2000) J. Biol. Chem. , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 43
    • 0038434056 scopus 로고    scopus 로고
    • A superfamily of protein tags: Ubiquitin, SUMO and related modifiers
    • D.C. Schwartz, and M. Hochstrasser A superfamily of protein tags: ubiquitin, SUMO and related modifiers Trends Biochem. Sci. 28 2003 321 328
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 321-328
    • Schwartz, D.C.1    Hochstrasser, M.2
  • 44
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • A.W. Segal How neutrophils kill microbes Annu. Rev. Immunol. 23 2005 197 223
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 197-223
    • Segal, A.W.1
  • 45
    • 31544477799 scopus 로고    scopus 로고
    • Pias1 interaction and sumoylation of metabotropic glutamate receptor 8
    • Z. Tang, O. El Far, H. Betz, and A. Scheschonka Pias1 interaction and sumoylation of metabotropic glutamate receptor 8 J. Biol. Chem. 280 2005 38153 38159
    • (2005) J. Biol. Chem. , vol.280 , pp. 38153-38159
    • Tang, Z.1    El Far, O.2    Betz, H.3    Scheschonka, A.4
  • 46
    • 23144449208 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins as multifunctional signals
    • R.L. Welchman, C. Gordon, and R.J. Mayer Ubiquitin and ubiquitin-like proteins as multifunctional signals Nat. Rev. Mol. Cell Biol. 6 2005 599 609
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 599-609
    • Welchman, R.L.1    Gordon, C.2    Mayer, R.J.3
  • 47
    • 0242668686 scopus 로고    scopus 로고
    • Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling
    • Z.A. Wood, L.B. Poole, and P.A. Karplus Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling Science 300 2003 650 653
    • (2003) Science , vol.300 , pp. 650-653
    • Wood, Z.A.1    Poole, L.B.2    Karplus, P.A.3
  • 48
    • 0037064080 scopus 로고    scopus 로고
    • Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid
    • K.S. Yang, S.W. Kang, H.A. Woo, S.C. Hwang, H.Z. Chae, K. Kim, and S.G. Rhee Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid J. Biol. Chem. 277 2002 38029 38036
    • (2002) J. Biol. Chem. , vol.277 , pp. 38029-38036
    • Yang, K.S.1    Kang, S.W.2    Woo, H.A.3    Hwang, S.C.4    Chae, H.Z.5    Kim, K.6    Rhee, S.G.7
  • 49
    • 3543018486 scopus 로고    scopus 로고
    • Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses
    • W. Zhou, J.J. Ryan, and H. Zhou Global analyses of sumoylated proteins in Saccharomyces cerevisiae. Induction of protein sumoylation by cellular stresses J. Biol. Chem. 279 2004 32262 32268
    • (2004) J. Biol. Chem. , vol.279 , pp. 32262-32268
    • Zhou, W.1    Ryan, J.J.2    Zhou, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.