A SIM-ultaneous role for SUMO and ubiquitin

Trends in Biochemical Sciences

Volumn 33, Issue 5, 2008, Pages 201-208

  Perry, J Jefferson P ^a,b   Tainer, John A ^a,c   Boddy, Michael N ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b AMRITA UNIVERSITY   (India)

^c LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

SUMO PROTEIN; SUMO TARGETED UBIQUITIN LIGASE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3;

CELL GROWTH; HOMEOSTASIS; HUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN STRUCTURE; REVIEW; SUMO INTERACTION MOTIF; SUMOYLATION; UBIQUITINATION;

AMINO ACID SEQUENCE; HUMANS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; NEOPLASM PROTEINS; NUCLEAR PROTEINS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN INTERACTION DOMAINS AND MOTIFS; SACCHAROMYCETALES; SEQUENCE ALIGNMENT; SMALL UBIQUITIN-RELATED MODIFIER PROTEINS; UBIQUITIN; UBIQUITIN-PROTEIN LIGASES;

EID: 43849093519     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2008.02.001     Document Type: Review

References (77)

1. Geiss-Friedlander R., and Melchior F. Concepts in sumoylation: a decade on. Nat. Rev. Mol. Cell Biol. 8 (2007) 947-956
2. Bayer P., et al. Structure determination of the small ubiquitin-related modifier SUMO-1. J. Mol. Biol. 280 (1998) 275-286
3. Vijay-Kumar S., et al. Structure of ubiquitin refined at 1.8 Å resolution. J. Mol. Biol. 194 (1987) 531-544
4. Huang T.T., and D'Andrea A.D. Regulation of DNA repair by ubiquitylation. Nat. Rev. Mol. Cell Biol. 7 (2006) 323-334
5. Gill G. SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?. Genes Dev. 18 (2004) 2046-2059
6. Ulrich H.D. Mutual interactions between the SUMO and ubiquitin systems: a plea of no contest. Trends Cell Biol. 15 (2005) 525-532
7. Anckar J., and Sistonen L. SUMO: getting it on. Biochem. Soc. Trans. 35 (2007) 1409-1413
8. Kerscher O., et al. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu. Rev. Cell Dev. Biol. 22 (2006) 159-180
9. 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 (2001) 35368-35374
10. Bylebyl G.R., et al. The SUMO isopeptidase Ulp2 prevents accumulation of SUMO chains in yeast. J. Biol. Chem. 278 (2003) 44113-44120
11. Cheng C.H., et al. SUMO modifications control assembly of synaptonemal complex and polycomplex in meiosis of Saccharomyces cerevisiae. Genes Dev. 20 (2006) 2067-2081
12. Takahashi Y., et al. A novel factor required for the SUMO1/Smt3 conjugation of yeast septins. Gene 275 (2001) 223-231
13. Borden K.L., et al. The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML. EMBO J. 14 (1995) 1532-1541
14. Saurin A.J., et al. Does this have a familiar RING?. Trends Biochem. Sci. 21 (1996) 208-214
15. Futreal P.A., et al. BRCA1 mutations in primary breast and ovarian carcinomas. Science 266 (1994) 120-122
16. Brzovic P.S., et al. Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 5646-5651
17. Buchwald G., et al. Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b. EMBO J. 25 (2006) 2465-2474
18. Kahyo T., et al. Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol. Cell 8 (2001) 713-718
19. Johnson E.S., and Gupta A.A. An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell 106 (2001) 735-744
20. Hochstrasser M. SP-RING for SUMO: new functions bloom for a ubiquitin-like protein. Cell 107 (2001) 5-8
21. Xhemalce B., et al. Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance. EMBO J. 23 (2004) 3844-3853
22. Sharrocks A.D. PIAS proteins and transcriptional regulation-more than just SUMO E3 ligases?. Genes Dev. 20 (2006) 754-758
23. Prudden J., et al. SUMO-targeted ubiquitin ligases in genome stability. EMBO J. 26 (2007) 4089-4101
24. Sun H., et al. Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins. EMBO J. 26 (2007) 4102-4112
25. Uzunova K., et al. Ubiquitin-dependent proteolytic control of SUMO conjugates. J. Biol. Chem. 282 (2007) 34167-34175
26. Xie Y., et al. The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation. J. Biol. Chem. 282 (2007) 34176-34184
27. Mullen J.R., et al. Requirement for three novel protein complexes in the absence of the Sgs1 DNA helicase in Saccharomyces cerevisiae. Genetics 157 (2001) 103-118
28. Brosh Jr. R.M., and Bohr V.A. Human premature aging, DNA repair and RecQ helicases. Nucleic Acids Res. 35 (2007) 7527-7544
29. Wang Z., et al. Genetic analysis connects SLX5 and SLX8 to the SUMO pathway in Saccharomyces cerevisiae. Genetics 172 (2006) 1499-1509
30. Kosoy A., et al. Fission yeast Rnf4 homologs are required for DNA repair. J. Biol. Chem. 282 (2007) 20388-20394
31. Pebernard S., et al. The Nse5-Nse6 dimer mediates DNA repair roles of the Smc5-Smc6 complex. Mol. Cell. Biol. 26 (2006) 1617-1630
32. Hazbun T.R., et al. Assigning function to yeast proteins by integration of technologies. Mol. Cell 12 (2003) 1353-1365
33. Murray A.W., and Kirschner M.W. Dominoes and clocks: the union of two views of the early embryonic cell cycle. Science 246 (1989) 614-621
34. Ii T., et al. Stimulation of in vitro sumoylation by Slx5-Slx8: evidence for a functional interaction with the SUMO pathway. DNA Repair (Amst.) 6 (2007) 1679-1691
35. Yang L., et al. Purification of the yeast Slx5-Slx8 protein complex and characterization of its DNA-binding activity. Nucleic Acids Res. 34 (2006) 5541-5551
36. Tu D., et al. Inaugural Article: Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 15599-15606
37. Ii T., et al. The yeast Slx5-Slx8 DNA integrity complex displays ubiquitin ligase activity. Cell Cycle 6 (2007) 2800-2809
38. Hecker C.M., et al. Specification of SUMO1- and SUMO2-interacting motifs. J. Biol. Chem. 281 (2006) 16117-16127
39. Shen T.H., et al. The mechanisms of PML-nuclear body formation. Mol. Cell 24 (2006) 331-339
40. Reverter D., and Lima C.D. Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature 435 (2005) 687-692
41. Song J., et al. Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 14373-14378
42. Hurley J.H., et al. Ubiquitin-binding domains. Biochem. J. 399 (2006) 361-372
43. Hicke L., et al. Ubiquitin-binding domains. Nat. Rev. Mol. Cell Biol. 6 (2005) 610-621
44. Burgess R.C., et al. The Slx5-Slx8 complex affects sumoylation of DNA repair proteins and negatively regulates recombination. Mol. Cell. Biol. 27 (2007) 6153-6162
45. Zhang C., et al. Suppression of genomic instability by SLX5 and SLX8 in Saccharomyces cerevisiae. DNA Repair (Amst.) 5 (2006) 336-346
46. Pichler A., et al. SUMO modification of the ubiquitin-conjugating enzyme E2-25K. Nat. Struct. Mol. Biol. 12 (2005) 264-269
47. Sobko A., et al. Regulated SUMOylation and ubiquitination of DdMEK1 is required for proper chemotaxis. Dev. Cell 2 (2002) 745-756
48. Bailey D., and O'Hare P. Comparison of the SUMO1 and ubiquitin conjugation pathways during the inhibition of proteasome activity with evidence of SUMO1 recycling. Biochem. J. 392 (2005) 271-281
49. Gill G. Something about SUMO inhibits transcription. Curr. Opin. Genet. Dev. 15 (2005) 536-541
50. Watts F.Z. The role of SUMO in chromosome segregation. Chromosoma 116 (2007) 15-20
51. Sacher M., et al. Control of Rad52 recombination activity by double-strand break-induced SUMO modification. Nat. Cell Biol. 8 (2006) 1284-1290
52. Boddy M.N., et al. Replication checkpoint kinase Cds1 regulates recombinational repair protein Rad60. Mol. Cell. Biol. 23 (2003) 5939-5946
53. Novatchkova M., et al. Proteins with two SUMO-like domains in chromatin-associated complexes: the RENi (Rad60-Esc2-NIP45) family. BMC Bioinformatics 6 (2005) 22
54. Raffa G.D., et al. SUMO-binding motifs mediate the Rad60-dependent response to replicative stress and self-association. J. Biol. Chem. 281 (2006) 27973-27981
55. Salghetti S.E., et al. Regulation of transcriptional activation domain function by ubiquitin. Science 293 (2001) 1651-1653
56. Beato M., et al. Steroid hormone receptors: many actors in search of a plot. Cell 83 (1995) 851-857
57. Tian S., et al. Small ubiquitin-related modifier-1 (SUMO-1) modification of the glucocorticoid receptor. Biochem. J. 367 (2002) 907-911
58. Poukka H., et al. Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 14145-14150
59. Abdel-Hafiz H., et al. The inhibitory function in human progesterone receptor N termini binds SUMO-1 protein to regulate autoinhibition and transrepression. J. Biol. Chem. 277 (2002) 33950-33956
60. Moilanen A.M., et al. Identification of a novel RING finger protein as a coregulator in steroid receptor-mediated gene transcription. Mol. Cell. Biol. 18 (1998) 5128-5139
61. Poukka H., et al. Coregulator small nuclear RING finger protein (SNURF) enhances Sp1- and steroid receptor-mediated transcription by different mechanisms. J. Biol. Chem. 275 (2000) 571-579
62. Nakajima A., et al. Ligand-dependent transcription of estrogen receptor α is mediated by the ubiquitin ligase EFP. Biochem. Biophys. Res. Commun. 357 (2007) 245-251
63. Cheng J., et al. SUMO-specific protease 1 is essential for stabilization of HIF1α during hypoxia. Cell 131 (2007) 584-595
64. Ulrich H.D. SUMO teams up with ubiquitin to manage hypoxia. Cell 131 (2007) 446-447
65. Rocha S. Gene regulation under low oxygen: holding your breath for transcription. Trends Biochem. Sci. 32 (2007) 389-397
66. Guan B., et al. Ubiquitination by TOPORS regulates the prostate tumor suppressor NKX3.1. J. Biol. Chem. 283 (2007) 4834-4840
67. Pungaliya P., et al. TOPORS functions as a SUMO-1 E3 ligase for chromatin-modifying proteins. J. Proteome Res. 6 (2007) 3918-3923
68. Rajendra R., et al. Topors functions as an E3 ubiquitin ligase with specific E2 enzymes and ubiquitinates p53. J. Biol. Chem. 279 (2004) 36440-36444
69. Desai S.D., et al. Ubiquitin, SUMO-1, and UCRP in camptothecin sensitivity and resistance. Ann. N. Y. Acad. Sci. 922 (2000) 306-308
70. Mao Y., et al. SUMO-1 conjugation to topoisomerase I: a possible repair response to topoisomerase-mediated DNA damage. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 4046-4051
71. Kim J.H., et al. Roles of sumoylation of a reptin chromatin-remodelling complex in cancer metastasis. Nat. Cell Biol. 8 (2006) 631-639
72. Steffan J.S., et al. SUMO modification of Huntingtin and Huntington's disease pathology. Science 304 (2004) 100-104
73. Pero R., et al. RNF4 is a growth inhibitor expressed in germ cells but not in human testicular tumors. Am. J. Pathol. 159 (2001) 1225-1230
74. Hirvonen-Santti S.J., et al. Down-regulation of estrogen receptor β and transcriptional coregulator SNURF/RNF4 in testicular germ cell cancer. Eur. Urol. 44 (2003) 742-747
75. Putnam C.D., et al. X-ray solution scattering (SAXS) combined with crystallography and computation: defining accurate macromolecular structures, conformations and assemblies in solution. Q. Rev. Biophys. 40 (2007) 191-285
76. Hitomi K., et al. The intricate structural chemistry of base excision repair machinery: implications for DNA damage recognition, removal, and repair. DNA Repair (Amst.) 6 (2007) 410-428
77. Song J., et al. Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. J. Biol. Chem. 280 (2005) 40122-40129