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Volumn 10, Issue 5, 2008, Pages 538-546

RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation

Author keywords

[No Author keywords available]

Indexed keywords

ARSENIC TRIOXIDE; PROMYELOCYTIC LEUKEMIA PROTEIN; PROTEASOME; RETINOIC ACID RECEPTOR ALPHA; RING FINGER PROTEIN; SMALL INTERFERING RNA; SUMO PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3;

EID: 43049093756     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1716     Document Type: Article
Times cited : (706)

References (29)
  • 1
    • 15944406765 scopus 로고    scopus 로고
    • A history of modification
    • Hay, R. T. SUMO: A history of modification. Mol. Cell 18, 1-12 (2005).
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.S.1
  • 2
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez, M. S., Dargemont, C. & Hay, R. T. SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J. Biol. Chem. 276, 12654-12659 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 3
    • 0035929557 scopus 로고    scopus 로고
    • Polymeric chains of sumo-2 and sumo-3 are conjugated to protein substrates by sae1/sae2 and ubc9
    • Tatham, M. H. et al. Polymeric chains of sumo-2 and sumo-3 are conjugated to protein substrates by sae1/sae2 and ubc9. J. Biol. Chem. 276, 35368-35374 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 35368-35374
    • Tatham, M.H.1
  • 4
    • 39049093685 scopus 로고    scopus 로고
    • In vivo identification of human SUM0 polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy
    • Matic, I. et al. In vivo identification of human SUM0 polymerization sites by high accuracy mass spectrometry and an in vitro to in vivo strategy. Mol. Cell Proteomics 1, 132-144 (2007).
    • (2007) Mol. Cell Proteomics , vol.1 , pp. 132-144
    • Matic, I.1
  • 7
    • 34648840192 scopus 로고    scopus 로고
    • SUMO-targeted ubiquitin ligases in genome stability
    • Prudden, J. et al. SUMO-targeted ubiquitin ligases in genome stability. EMBO J. 26, 4089-101. (2007).
    • (2007) EMBO J , vol.26 , pp. 4089-4101
    • Prudden, J.1
  • 8
    • 34648816891 scopus 로고    scopus 로고
    • Conserved function of RNF4 family proteins in eukaryotes: Targetinga ubiquitin ligase to SUMOylated proteins
    • Sun, H., Leverson, J. D. & Hunter, T. Conserved function of RNF4 family proteins in eukaryotes: Targetinga ubiquitin ligase to SUMOylated proteins. EMBO J. 26, 4102-4112 (2007).
    • (2007) EMBO J , vol.26 , pp. 4102-4112
    • Sun, H.1    Leverson, J.D.2    Hunter, T.3
  • 9
    • 36348977099 scopus 로고    scopus 로고
    • Ubiquitin-dependent proteolytic control of SUM0 conjugates
    • Uzunova, K. et al. Ubiquitin-dependent proteolytic control of SUM0 conjugates. J. Biol. Chem. 47, 34167-34175 (2007).
    • (2007) J. Biol. Chem , vol.47 , pp. 34167-34175
    • Uzunova, K.1
  • 10
    • 36348964395 scopus 로고    scopus 로고
    • The yeast HEX3-SLX8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation
    • Xie, Y. et al. The yeast HEX3-SLX8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation. J. Biol. Chem. 47 34176-34184 (2007).
    • (2007) J. Biol. Chem , vol.47 , pp. 34176-34184
    • Xie, Y.1
  • 11
    • 0031812159 scopus 로고    scopus 로고
    • Identification of a novel RING finger protein as a co-regulator in steroid receptor-mediated gene transcription
    • Moilanen, A. M. et al. Identification of a novel RING finger protein as a co-regulator in steroid receptor-mediated gene transcription. Mol. Cell Biol. 18, 5128-5139 (1998).
    • (1998) Mol. Cell Biol , vol.18 , pp. 5128-5139
    • Moilanen, A.M.1
  • 12
    • 1342265499 scopus 로고    scopus 로고
    • Transcriptional co-regulator SNURF (RNF4) possesses ubiquitin E3 ligase activity
    • Hakli, M., Lorick, K. L., Weissman, A. M., Janne, O. A. & Palvimo. J. J. Transcriptional co-regulator SNURF (RNF4) possesses ubiquitin E3 ligase activity. FEBS Lett. 560, 56-62 (2004).
    • (2004) FEBS Lett , vol.560 , pp. 56-62
    • Hakli, M.1    Lorick, K.L.2    Weissman, A.M.3    Janne, O.A.4    Palvimo, J.J.5
  • 13
    • 0012351964 scopus 로고    scopus 로고
    • Properties of 13C-substituted arginine in stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong, S. E., Kratchmarova, I. & Mann, M. Properties of 13C-substituted arginine in stable isotope labeling by amino acids in cell culture (SILAC). J Proteome Res. 2, 173-181 (2003).
    • (2003) J Proteome Res , vol.2 , pp. 173-181
    • Ong, S.E.1    Kratchmarova, I.2    Mann, M.3
  • 14
    • 0010740572 scopus 로고    scopus 로고
    • In vitro studies on cellular and molecular mechanisms of arsenic trioxide (As2O3) in the treatment of acute promyelocytic leukemia: As2O3 induces NB4 cell apoptosis with downregulation of Bcl-2 expression and modulation of PML-RAR α/PML proteins
    • Chen, G. Q. et al. In vitro studies on cellular and molecular mechanisms of arsenic trioxide (As2O3) in the treatment of acute promyelocytic leukemia: As2O3 induces NB4 cell apoptosis with downregulation of Bcl-2 expression and modulation of PML-RAR α/PML proteins. Blood 88, 1052-1061 (1996).
    • (1996) Blood , vol.88 , pp. 1052-1061
    • Chen, G.Q.1
  • 15
    • 0035908032 scopus 로고    scopus 로고
    • Role oi promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3 induced PML or PML/retinoic acid receptor alpha degradation
    • Lallemand-Breitenbach, V. et al. Role oi promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3 induced PML or PML/retinoic acid receptor alpha degradation. J. Exp. Med. 193, 1361-1371 (2001).
    • (2001) J. Exp. Med , vol.193 , pp. 1361-1371
    • Lallemand-Breitenbach, V.1
  • 16
    • 0032402135 scopus 로고    scopus 로고
    • Trivalent antimonials induce legradation of the PML-RAR oncoprotein and reorganization of the promyelocytic leukemia nuclear bodies in acute promyelocytic leukemia NB4 cells
    • Muller, S., Miller, W. H., Jr & Dejean, A. Trivalent antimonials induce legradation of the PML-RAR oncoprotein and reorganization of the promyelocytic leukemia nuclear bodies in acute promyelocytic leukemia NB4 cells. Blood 92, 4308-4316 (1998).
    • (1998) Blood , vol.92 , pp. 4308-4316
    • Muller, S.1    Miller Jr, W.H.2    Dejean, A.3
  • 17
    • 0000531696 scopus 로고    scopus 로고
    • Arsenic trioxide as an inducer of apoptosis and loss of PML/RAR α protein in acute prorayelocytic leukemia cells
    • Shao, W. et al. Arsenic trioxide as an inducer of apoptosis and loss of PML/RAR α protein in acute prorayelocytic leukemia cells. J. Natl Cancer Inst. 90, 124-133 (1998).
    • (1998) J. Natl Cancer Inst , vol.90 , pp. 124-133
    • Shao, W.1
  • 18
    • 0033037274 scopus 로고    scopus 로고
    • PIC-1/SUMO-1-modified PML-retinoic acid receptor a mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia
    • Sternsdorf, T. et al. PIC-1/SUMO-1-modified PML-retinoic acid receptor a mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia. Mol. Cell Biol. 19, 5170-5178 (1999).
    • (1999) Mol. Cell Biol , vol.19 , pp. 5170-5178
    • Sternsdorf, T.1
  • 19
    • 0030890942 scopus 로고    scopus 로고
    • Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia
    • Zhu, J. et al. Arsenic-induced PML targeting onto nuclear bodies: implications for the treatment of acute promyelocytic leukemia. Proc. Natl Acad. Sci. USA 94, 3978-3983 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 3978-3983
    • Zhu, J.1
  • 20
    • 0033034749 scopus 로고    scopus 로고
    • SUMO-1 modification of the acute promyelocytic leukaemia protein PML: Implications for nuclear localisation
    • Duprez, E. et al. SUMO-1 modification of the acute promyelocytic leukaemia protein PML: Implications for nuclear localisation. J. Cell Sci. 112, 381-393 (1999).
    • (1999) J. Cell Sci , vol.112 , pp. 381-393
    • Duprez, E.1
  • 21
    • 0032500634 scopus 로고    scopus 로고
    • Identification of three major sentrinization sites in PML
    • Kamitani, T. et al. Identification of three major sentrinization sites in PML. J. Biol. Chem. 273, 26675-26682 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 26675-26682
    • Kamitani, T.1
  • 22
    • 34548213631 scopus 로고    scopus 로고
    • The slx5-slx8 complex affects sumoylation of DNA repair proteins and negatively regulates recombination
    • Burgess, R. C., Rahman, S., Lisby, M., Rothstein, R. & Zhao, X. The slx5-slx8 complex affects sumoylation of DNA repair proteins and negatively regulates recombination. Mol. Cell Biol. 27, 6153-6162 (2007).
    • (2007) Mol. Cell Biol , vol.27 , pp. 6153-6162
    • Burgess, R.C.1    Rahman, S.2    Lisby, M.3    Rothstein, R.4    Zhao, X.5
  • 23
    • 34547136728 scopus 로고    scopus 로고
    • Fission yeast Rnf4 homologs are required for DNA repair
    • Kosoy, A., Calonge, T. M., Outwin, E. A. & O'Connell, M. J. Fission yeast Rnf4 homologs are required for DNA repair. J. Biol. Chem. 282, 20388-20394 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 20388-20394
    • Kosoy, A.1    Calonge, T.M.2    Outwin, E.A.3    O'Connell, M.J.4
  • 24
    • 33645222457 scopus 로고    scopus 로고
    • Genetic analysis connects SLX5 and SLX8 to the SUM0 pathway in Saccharomyces ceirevisiae
    • Wang, Z., Jones, G. M. & Prelich, G. Genetic analysis connects SLX5 and SLX8 to the SUM0 pathway in Saccharomyces ceirevisiae. Genetics 172, 1499-1509 (2006).
    • (2006) Genetics , vol.172 , pp. 1499-1509
    • Wang, Z.1    Jones, G.M.2    Prelich, G.3
  • 25
    • 13544254439 scopus 로고    scopus 로고
    • SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies
    • Hakli, M., Karvonen, U., Janne, O. A. & Palvimo, J. J. SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies. Exp. Cell Res. 304, 224-233 (2005).
    • (2005) Exp. Cell Res , vol.304 , pp. 224-233
    • Hakli, M.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 26
    • 0032420269 scopus 로고    scopus 로고
    • An improved PCR-based method forsite directed mutagenesis using megaprimers
    • Brons-Poulsen, J., Petersen, N. E., Horder, M. & Kristiansen, K. An improved PCR-based method forsite directed mutagenesis using megaprimers. Mol. Cell Probes 12, 345-348 (1998).
    • (1998) Mol. Cell Probes , vol.12 , pp. 345-348
    • Brons-Poulsen, J.1    Petersen, N.E.2    Horder, M.3    Kristiansen, K.4
  • 27
    • 33845372240 scopus 로고    scopus 로고
    • SUMO protease SENPI induces isomerization of the scissile peptide bond
    • Shen, L. et al. SUMO protease SENPI induces isomerization of the scissile peptide bond. Nature Struct. Mol. Biol. 13, 1069-1077 (2006).
    • (2006) Nature Struct. Mol. Biol , vol.13 , pp. 1069-1077
    • Shen, L.1
  • 28
    • 0030728212 scopus 로고    scopus 로고
    • Ubch9 conjugates SUMO but not ubiquitin
    • Desterro, J. M., Thomson, J. & Hay, R. T. Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett. 417, 297-300 (1997).
    • (1997) FEBS Lett , vol.417 , pp. 297-300
    • Desterro, J.M.1    Thomson, J.2    Hay, R.T.3
  • 29
    • 33746038148 scopus 로고    scopus 로고
    • The structure of SENP1- SUMO-2 complex suggests a structural basis for discrimination between SUM0 paralogues during processing
    • Shen, L. N., Dong, C., Liu, H., Naismith, J. H. & Hay, R. T. The structure of SENP1- SUMO-2 complex suggests a structural basis for discrimination between SUM0 paralogues during processing. Biochem. J. 397, 279-288 (2006).
    • (2006) Biochem. J , vol.397 , pp. 279-288
    • Shen, L.N.1    Dong, C.2    Liu, H.3    Naismith, J.H.4    Hay, R.T.5


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