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Volumn 43, Issue 1, 2011, Pages 37-40

Small ubiquitin-related modifier-1: Wrestling with protein regulation

Author keywords

Protein modification; SUMO; Ubiquitin

Indexed keywords

SUMO 1 PROTEIN;

EID: 78650234937     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2010.09.022     Document Type: Short Survey
Times cited : (10)

References (30)
  • 3
    • 0029736651 scopus 로고    scopus 로고
    • PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • M.N. Boddy, K. Howe, L.D. Etkin, E. Solomon, and P.S. Freemont PIC 1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia Oncogene 13 1996 971 982
    • (1996) Oncogene , vol.13 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 4
    • 3042644131 scopus 로고    scopus 로고
    • A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type i diabetes mellitus
    • K.M. Bohren, V. Nadkarni, J.H. Song, K.H. Gabbay, and D. Owerbach A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus J Biol Chem 279 2004 27233 27238
    • (2004) J Biol Chem , vol.279 , pp. 27233-27238
    • Bohren, K.M.1    Nadkarni, V.2    Song, J.H.3    Gabbay, K.H.4    Owerbach, D.5
  • 5
    • 0032433265 scopus 로고    scopus 로고
    • Characterization of mouse ubiquitin-like SMT3A and SMT3B cDNAs and gene/pseudogenes
    • A. Chen, H. Mannen, and S.S. Li Characterization of mouse ubiquitin-like SMT3A and SMT3B cDNAs and gene/pseudogenes Biochem Mol Biol Int 46 1998 1161 1174
    • (1998) Biochem Mol Biol Int , vol.46 , pp. 1161-1174
    • Chen, A.1    Mannen, H.2    Li, S.S.3
  • 6
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation
    • J.M. Desterro, M.S. Rodriguez, and R.T. Hay SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation Mol Cell 2 1998 233 239
    • (1998) Mol Cell , vol.2 , pp. 233-239
    • Desterro, J.M.1    Rodriguez, M.S.2    Hay, R.T.3
  • 7
    • 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
  • 9
    • 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
  • 10
    • 0032567759 scopus 로고    scopus 로고
    • Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association
    • R. Mahajan, L. Gerace, and F. Melchior Molecular characterization of the SUMO-1 modification of RanGAP1 and its role in nuclear envelope association J Cell Biol 140 1998 259 270
    • (1998) J Cell Biol , vol.140 , pp. 259-270
    • Mahajan, R.1    Gerace, L.2    Melchior, F.3
  • 11
    • 55249095331 scopus 로고    scopus 로고
    • Phosphorylation of SUMO-1 occurs in vivo and is conserved through evolution
    • I. Matic, B. Macek, M. Hilger, T.C. Walther, and M. Mann Phosphorylation of SUMO-1 occurs in vivo and is conserved through evolution J Proteome Res 7 2008 4050 4057
    • (2008) J Proteome Res , vol.7 , pp. 4050-4057
    • Matic, I.1    MacEk, B.2    Hilger, M.3    Walther, T.C.4    Mann, M.5
  • 12
    • 39049093685 scopus 로고    scopus 로고
    • In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy
    • I. Matic, M. van Hagen, J. Schimmel, B. Macek, S.C. Ogg, and M.H. Tatham In vivo identification of human small ubiquitin-like modifier polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy Mol Cell Proteomics 7 2008 132 144
    • (2008) Mol Cell Proteomics , vol.7 , pp. 132-144
    • Matic, I.1    Van Hagen, M.2    Schimmel, J.3    MacEk, B.4    Ogg, S.C.5    Tatham, M.H.6
  • 13
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • M.J. Matunis, E. Coutavas, and G. Blobel A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex J Cell Biol 135 1996 1457 1470
    • (1996) J Cell Biol , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 14
    • 0036554867 scopus 로고    scopus 로고
    • Differential gene expression in human lung adenocarcinomas and squamous cell carcinomas
    • A.L. McDoniels-Silvers, C.F. Nimri, G.D. Stoner, R.A. Lubet, and M. You Differential gene expression in human lung adenocarcinomas and squamous cell carcinomas Clin Cancer Res 8 2002 1127 1138
    • (2002) Clin Cancer Res , vol.8 , pp. 1127-1138
    • McDoniels-Silvers, A.L.1    Nimri, C.F.2    Stoner, G.D.3    Lubet, R.A.4    You, M.5
  • 16
    • 72449163470 scopus 로고    scopus 로고
    • The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress
    • J.R. Morris, C. Boutell, M. Keppler, R. Densham, D. Weekes, and A. Alamshah The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress Nature 462 2009 886 890
    • (2009) Nature , vol.462 , pp. 886-890
    • Morris, J.R.1    Boutell, C.2    Keppler, M.3    Densham, R.4    Weekes, D.5    Alamshah, A.6
  • 17
    • 32144463131 scopus 로고    scopus 로고
    • Genetic analysis of BRCA1 ubiquitin ligase activity and its relationship to breast cancer susceptibility
    • J.R. Morris, L. Pangon, C. Boutell, T. Katagiri, N.H. Keep, and E. Solomon Genetic analysis of BRCA1 ubiquitin ligase activity and its relationship to breast cancer susceptibility Hum Mol Genet 15 2006 599 606
    • (2006) Hum Mol Genet , vol.15 , pp. 599-606
    • Morris, J.R.1    Pangon, L.2    Boutell, C.3    Katagiri, T.4    Keep, N.H.5    Solomon, E.6
  • 18
    • 0030588674 scopus 로고    scopus 로고
    • Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin
    • T. Okura, L. Gong, T. Kamitani, T. Wada, I. Okura, and C.F. Wei Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin J Immunol 157 1996 4277 4281
    • (1996) J Immunol , vol.157 , pp. 4277-4281
    • Okura, T.1    Gong, L.2    Kamitani, T.3    Wada, T.4    Okura, I.5    Wei, C.F.6
  • 19
    • 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
  • 20
    • 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
  • 21
    • 63549136610 scopus 로고    scopus 로고
    • Sumoylation and human disease pathogenesis
    • K.D. Sarge, and O.K. Park-Sarge Sumoylation and human disease pathogenesis Trends Biochem Sci 34 2009 200 205
    • (2009) Trends Biochem Sci , vol.34 , pp. 200-205
    • Sarge, K.D.1    Park-Sarge, O.K.2
  • 23
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins
    • W. Seufert, B. Futcher, and S. Jentsch Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins Nature 373 1995 78 81
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert, W.1    Futcher, B.2    Jentsch, S.3
  • 24
    • 0030249870 scopus 로고    scopus 로고
    • UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins
    • Z. Shen, P.E. Pardington-Purtymun, J.C. Comeaux, R.K. Moyzis, and D.J. Chen UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins Genomics 36 1996 271 279
    • (1996) Genomics , vol.36 , pp. 271-279
    • Shen, Z.1    Pardington-Purtymun, P.E.2    Comeaux, J.C.3    Moyzis, R.K.4    Chen, D.J.5
  • 26
    • 0033037274 scopus 로고    scopus 로고
    • PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia
    • T. Sternsdorf, E. Puccetti, K. Jensen, D. Hoelzer, H. Will, and O.G. Ottmann PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia Mol Cell Biol 19 1999 5170 5178
    • (1999) Mol Cell Biol , vol.19 , pp. 5170-5178
    • Sternsdorf, T.1    Puccetti, E.2    Jensen, K.3    Hoelzer, D.4    Will, H.5    Ottmann, O.G.6
  • 27
    • 0037151769 scopus 로고    scopus 로고
    • Molecular features of human ubiquitin-like SUMO genes and their encoded proteins
    • H.L. Su, and S.S. Li Molecular features of human ubiquitin-like SUMO genes and their encoded proteins Gene 296 2002 65 73
    • (2002) Gene , vol.296 , pp. 65-73
    • Su, H.L.1    Li, S.S.2
  • 28
    • 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
  • 30
    • 47549109045 scopus 로고    scopus 로고
    • Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies
    • Y.Q. Zhang, and K.D. Sarge Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies J Cell Biol 182 2008 35 39
    • (2008) J Cell Biol , vol.182 , pp. 35-39
    • Zhang, Y.Q.1    Sarge, K.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.