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Volumn 457, Issue 3, 2014, Pages 435-440

SIM-dependent enhancement of substrate-specific SUMOylation by a ubiquitin ligase in vitro

Author keywords

Proliferating cell nuclear antigen (PCNA); Radiation sensitive 18 (Rad18); Small ubiquitin related modifier(SUMO); SUMO interaction motif (SIM); SUMO targeted ubiquitin ligase (STUbL); Ubiquitin

Indexed keywords

CYCLINE; PROTEIN UBC9; RAD18 PROTEIN; SUMO PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

EID: 84892156653     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20131381     Document Type: Article
Times cited : (15)

References (39)
  • 1
  • 3
    • 84858135252 scopus 로고    scopus 로고
    • Following Ariadne's thread: A new perspective on RBR ubiquitin ligases
    • Wenzel, D. M. and Klevit, R. E. (2012) Following Ariadne's thread: a new perspective on RBR ubiquitin ligases. BMC Biol. 10, 24
    • (2012) BMC Biol. , vol.10 , pp. 24
    • Wenzel, D.M.1    Klevit, R.E.2
  • 4
    • 44949231368 scopus 로고    scopus 로고
    • Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling
    • Li, W., Bengtson, M. H., Ulbrich, A., Matsuda, A., Reddy, V. A., Orth, A., Chanda, S. K., Batalov, S. and Joazeiro, C. A. (2008) Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling. PLoS ONE 3, e1487
    • (2008) PLoS ONE , vol.3
    • Li, W.1    Bengtson, M.H.2    Ulbrich, A.3    Matsuda, A.4    Reddy, V.A.5    Orth, A.6    Chanda, S.K.7    Batalov, S.8    Joazeiro, C.A.9
  • 5
    • 84878944582 scopus 로고    scopus 로고
    • Sumoylation: A regulatory protein modification in health and disease
    • Flotho, A. and Melchior, F. (2013) Sumoylation: a regulatory protein modification in health and disease. Annu. Rev. Biochem. 82, 357-385
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 6
    • 0037068455 scopus 로고    scopus 로고
    • RAD6 -dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • Hoege, C., Pfander, B., Moldovan, G. L., Pyrowolakis, G. and Jentsch, S. (2002) RAD6 -dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 419, 135-141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 7
    • 0141831006 scopus 로고    scopus 로고
    • Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
    • Stelter, P. and Ulrich, H. D. (2003) Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature 425, 188-191
    • (2003) Nature , vol.425 , pp. 188-191
    • Stelter, P.1    Ulrich, H.D.2
  • 8
    • 63049106529 scopus 로고    scopus 로고
    • Regulating post-translational modifications of the eukaryotic replication clamp PCNA
    • Ulrich, H. D. (2009) Regulating post-translational modifications of the eukaryotic replication clamp PCNA. DNA Repair 8, 461-469
    • (2009) DNA Repair , vol.8 , pp. 461-469
    • Ulrich, H.D.1
  • 9
    • 78649451521 scopus 로고    scopus 로고
    • RAD18 lives a double life: Its implication in DNA double-strand break repair
    • Ting, L., Jun, H. and Junjie, C. (2010) RAD18 lives a double life: its implication in DNA double-strand break repair. DNA Repair 9, 1241-1248
    • (2010) DNA Repair , vol.9 , pp. 1241-1248
    • Ting, L.1    Jun, H.2    Junjie, C.3
  • 10
    • 0034730134 scopus 로고    scopus 로고
    • Functions of the DNA damage response pathway target Ho endonuclease of yeast for degradation via the ubiquitin-26S proteasome system
    • Kaplun, L., Ivantsiv, Y., Kornitzer, D. and Raveh, D. (2000) Functions of the DNA damage response pathway target Ho endonuclease of yeast for degradation via the ubiquitin-26S proteasome system. Proc. Natl. Acad. Sci. U.S.A. 97, 10077-10082
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 10077-10082
    • Kaplun, L.1    Ivantsiv, Y.2    Kornitzer, D.3    Raveh, D.4
  • 11
    • 40649097306 scopus 로고    scopus 로고
    • Activation of ubiquitin-dependent DNA damage bypass is mediated by Replication Protein a
    • Davies, A. A., Huttner, D., Daigaku, Y., Chen, S. and Ulrich, H. D. (2008) Activation of ubiquitin-dependent DNA damage bypass is mediated by Replication Protein A. Mol. Cell 29, 625-636
    • (2008) Mol. Cell , vol.29 , pp. 625-636
    • Davies, A.A.1    Huttner, D.2    Daigaku, Y.3    Chen, S.4    Ulrich, H.D.5
  • 13
    • 84871206469 scopus 로고    scopus 로고
    • A SUMO-interacting motif activates budding yeast ubiquitin ligase Rad18 towards SUMO-modified PCNA
    • Parker, J. L. and Ulrich, H. D. (2012) A SUMO-interacting motif activates budding yeast ubiquitin ligase Rad18 towards SUMO-modified PCNA. Nucleic Acids Res. 40, 11380-11388
    • (2012) Nucleic Acids Res. , vol.40 , pp. 11380-11388
    • Parker, J.L.1    Ulrich, H.D.2
  • 14
  • 15
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., Halladay, J. and Craig, E. A. (1996) Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144, 1425-1436
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 16
    • 0034600851 scopus 로고    scopus 로고
    • Two RING finger proteins mediate cooperation between ubiquitin- conjugating enzymes in DNA repair
    • Ulrich, H. D. and Jentsch, S. (2000) Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. EMBO J. 19, 3388-3397
    • (2000) EMBO J. , vol.19 , pp. 3388-3397
    • Ulrich, H.D.1    Jentsch, S.2
  • 18
    • 38049079191 scopus 로고    scopus 로고
    • Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae
    • Windecker, H. and Ulrich, H. D. (2008) Architecture and assembly of poly-SUMO chains on PCNA in Saccharomyces cerevisiae. J. Mol. Biol. 376, 221-231
    • (2008) J. Mol. Biol. , vol.376 , pp. 221-231
    • Windecker, H.1    Ulrich, H.D.2
  • 19
    • 0028314007 scopus 로고
    • Specific complex formation between yeast RAD6 and RAD18 proteins: A potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites
    • Bailly, V., Lamb, J., Sung, P., Prakash, S. and Prakash, L. (1994) Specific complex formation between yeast RAD6 and RAD18 proteins: a potential mechanism for targeting RAD6 ubiquitin-conjugating activity to DNA damage sites. Genes Dev. 8, 811-820
    • (1994) Genes Dev. , vol.8 , pp. 811-820
    • Bailly, V.1    Lamb, J.2    Sung, P.3    Prakash, S.4    Prakash, L.5
  • 21
    • 0030791425 scopus 로고    scopus 로고
    • Domains required for dimerization of yeast Rad6 ubiquitin-conjugating enzyme and Rad18 DNA binding protein
    • Bailly, V., Prakash, S. and Prakash, L. (1997) Domains required for dimerization of yeast Rad6 ubiquitin-conjugating enzyme and Rad18 DNA binding protein. Mol. Cell. Biol. 17, 4536-4543
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4536-4543
    • Bailly, V.1    Prakash, S.2    Prakash, L.3
  • 23
    • 35348982302 scopus 로고    scopus 로고
    • Stimulation of in vitro sumoylation by Slx5-Slx8: Evidence for a functional interaction with the SUMO pathway
    • Ii, T., Mullen, J. R., Slagle, C. E. and Brill, S. J. (2007) Stimulation of in vitro sumoylation by Slx5-Slx8: evidence for a functional interaction with the SUMO pathway. DNA Repair 6, 1679-1691
    • (2007) DNA Repair , vol.6 , pp. 1679-1691
    • Ii, T.1    Mullen, J.R.2    Slagle, C.E.3    Brill, S.J.4
  • 24
    • 34250375116 scopus 로고    scopus 로고
    • E3-independent monoubiquitination of ubiquitin-binding proteins
    • Hoeller, D., Hecker, C. M., Wagner, S., Rogov, V., Dotsch, V. and Dikic, I. (2007) E3-independent monoubiquitination of ubiquitin-binding proteins. Mol. Cell 26, 891-898
    • (2007) Mol. Cell , vol.26 , pp. 891-898
    • Hoeller, D.1    Hecker, C.M.2    Wagner, S.3    Rogov, V.4    Dotsch, V.5    Dikic, I.6
  • 26
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein Pc2 is a SUMO E3
    • Kagey, M. H., Melhuish, T. A. and Wotton, D. (2003) The polycomb protein Pc2 is a SUMO E3. Cell 113, 127-137
    • (2003) Cell , vol.113 , pp. 127-137
    • Kagey, M.H.1    Melhuish, T.A.2    Wotton, D.3
  • 27
    • 77950643586 scopus 로고    scopus 로고
    • The SUMO E3 ligase activity of Pc2 is coordinated through a SUMO interaction motif
    • Yang, S. H. and Sharrocks, A. D. (2010) The SUMO E3 ligase activity of Pc2 is coordinated through a SUMO interaction motif. Mol. Cell. Biol. 30, 2193-2205
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 2193-2205
    • Yang, S.H.1    Sharrocks, A.D.2
  • 29
    • 24144483441 scopus 로고    scopus 로고
    • Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo
    • Weger, S., Hammer, E. and Heilbronn, R. (2005) Topors acts as a SUMO-1 E3 ligase for p53 in vitro and in vivo. FEBS Lett. 579, 5007-5012
    • (2005) FEBS Lett. , vol.579 , pp. 5007-5012
    • Weger, S.1    Hammer, E.2    Heilbronn, R.3
  • 30
    • 67650076601 scopus 로고    scopus 로고
    • MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission
    • Braschi, E., Zunino, R. and McBride, H. M. (2009) MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission. EMBO Rep. 10, 748-754
    • (2009) EMBO Rep. , vol.10 , pp. 748-754
    • Braschi, E.1    Zunino, R.2    McBride, H.M.3
  • 31
    • 79952096721 scopus 로고    scopus 로고
    • Evidence implicating CCNB1IP1, a RING domain-containing protein required for meiotic crossing over in mice, as an E3 SUMO ligase
    • Strong, E. R. and Schimenti, J. C. (2010) Evidence implicating CCNB1IP1, a RING domain-containing protein required for meiotic crossing over in mice, as an E3 SUMO ligase. Genes 1, 440-451
    • (2010) Genes , vol.1 , pp. 440-451
    • Strong, E.R.1    Schimenti, J.C.2
  • 32
    • 79952281303 scopus 로고    scopus 로고
    • SUMO E3 ligase activity of TRIM proteins
    • Chu, Y. and Yang, X. (2011) SUMO E3 ligase activity of TRIM proteins. Oncogene 30, 1108-1116
    • (2011) Oncogene , vol.30 , pp. 1108-1116
    • Chu, Y.1    Yang, X.2
  • 33
    • 19644384513 scopus 로고    scopus 로고
    • Sumoylation induced by the Arf tumor suppressor: A p53-independent function
    • Tago, K., Chiocca, S. and Sherr, C. J. (2005) Sumoylation induced by the Arf tumor suppressor: a p53-independent function. Proc. Natl. Acad. Sci. U.S.A. 102, 7689-7694
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 7689-7694
    • Tago, K.1    Chiocca, S.2    Sherr, C.J.3
  • 35
    • 77149134314 scopus 로고    scopus 로고
    • Ebp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity
    • Oh, S. M., Liu, Z., Okada, M., Jang, S. W., Liu, X., Chan, C. B., Luo, H. and Ye, K. (2010) Ebp1 sumoylation, regulated by TLS/FUS E3 ligase, is required for its anti-proliferative activity. Oncogene 29, 1017-1030
    • (2010) Oncogene , vol.29 , pp. 1017-1030
    • Oh, S.M.1    Liu, Z.2    Okada, M.3    Jang, S.W.4    Liu, X.5    Chan, C.B.6    Luo, H.7    Ye, K.8
  • 37
    • 84856101167 scopus 로고    scopus 로고
    • The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G1 arrest
    • Bennett, R. L., Pan, Y., Christian, J., Hui, T. and May, Jr, W. S. (2012) The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and activation, leading to G1 arrest. Cell Cycle 11, 407-417
    • (2012) Cell Cycle , vol.11 , pp. 407-417
    • Bennett, R.L.1    Pan, Y.2    Christian, J.3    Hui, T.4    May Jr., W.S.5


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