SUMO: Ligases, isopeptidases and nuclear pores

Trends in Biochemical Sciences

Volumn 28, Issue 11, 2003, Pages 612-618

  Melchior, Frauke ^a   Schergaut, Marion ^a   Pichler, Andrea ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ISOENZYME; LIGASE; NUCLEOPORIN 358; PC2 PROTEIN; PEPTIDASE; PROTEIN; PROTEIN INHIBITOR OF ACTIVATED STAT; RAN PROTEIN; SUMO PROTEIN; UNCLASSIFIED DRUG;

CONJUGATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME LOCALIZATION; ENZYME MODIFICATION; ENZYME STABILITY; HUMAN; NONHUMAN; NUCLEAR PORE; NUCLEOCYTOPLASMIC TRANSPORT; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT; REGULATORY MECHANISM; REVIEW;

ACTIVE TRANSPORT, CELL NUCLEUS; ANIMALS; CARBON-NITROGEN LYASES; HUMANS; NUCLEAR PORE; NUCLEAR PORE COMPLEX PROTEINS; SMALL UBIQUITIN-RELATED MODIFIER PROTEINS; UBIQUITIN-PROTEIN LIGASES;

EID: 1542501958     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2003.09.002     Document Type: Review

References (64)

1. Melchior F. SUMO - nonclassical ubiquitin. Annu. Rev. Cell Dev. Biol. 16:2000;591-626.
2. Muller S., et al. SUMO, ubiquitin's mysterious cousin. Nat. Rev. Mol. Cell Biol. 2:2001;202-210.
3. Kim K.I., et al. Versatile protein tag, SUMO: its enzymology and biological function. J. Cell. Physiol. 191:2002;257-268.
4. Schwarz D.C., Hochstrasser M. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem. Sci. 28:2003;321-328.
5. Saitoh H., Hinchey J. Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J. Biol. Chem. 275:2000;6252-6258.
6. Kurepa J., et al. The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by stress. J. Biol. Chem. 278:2003;6862-6872.
7. Seeler J.S., Dejean A. SUMO: of branched proteins and nuclear bodies. Oncogene. 20:2001;7243-7249.
8. Alarcon-Vargas D., Ronai Z. SUMO in cancer-wrestlers wanted. Cancer Biol. Ther. 1:2002;237-242.
9. Wilson V.G., Rangasamy D. Viral interaction with the host cell sumoylation system. Virus Res. 81:2001;17-27.
10. Pichler A., Melchior F. Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport. Traffic. 3:2002;381-387.
11. Gill G. 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.
12. Verger A., et al. Modification with SUMO. EMBO Rep. 4:2003;137-142.
13. Sobko A., et al. Regulated sumoylation and ubiquitination of DdMEK1 is required for proper chemotaxis. Dev. Cell. 2:2002;745-756.
14. Hoege C., et al. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature. 419:2002;135-141.
15. Bernier-Villamor V., et al. Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1. Cell. 108:2002;345-356.
16. Lee P.S., et al. Sumoylation of Smad4, the common Smad mediator of transforming growth factor-β family signaling. J. Biol. Chem. 278:2003;27853-27863.
17. Lin X., et al. Activation of transforming growth factor-β signaling by SUMO-1 modification of tumor suppressor Smad4/DPC4. J. Biol. Chem. 278:2003;18714-18719.
18. 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.
19. Pichler A., et al. The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell. 108:2002;109-120.
20. Hochstrasser M. SP-RING for SUMO: new functions bloom for a ubiquitin-like protein. Cell. 107:2001;5-8.
21. Jackson P.K. A new RING for SUMO: wrestling transcriptional responses into nuclear bodies with PIAS family E3 SUMO ligases. Genes Dev. 15:2001;3053-3058.
22. Johnson E.S., Gupta A.A. An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell. 106:2001;735-744.
23. Takahashi Y., et al. Yeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates. J. Biol. Chem. 276:2001;48973-48977.
24. Kagey M.H., et al. The Polycomb protein Pc2 is a SUMO E3. Cell. 113:2003;127-137.
25. Lin X., et al. Opposed regulation of corepressor CtBP by sumoylation and PDZ binding. Mol. Cell. 11:2003;1389-1396.
26. Schmidt D., Muller S. Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity. Proc. Natl. Acad. Sci. U. S. A. 99:2002;2872-2877.
27. Li S.J., Hochstrasser M. A new protease required for cell-cycle progression in yeast. Nature. 398:1999;246-251.
28. Li S.J., Hochstrasser M. The Ulp1 SUMO isopeptidase: distinct domains required for viability, nuclear envelope localization, and substrate specificity. J. Cell Biol. 160:2003;1069-1082.
29. Li S.J., Hochstrasser M. The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein. Mol. Cell. Biol. 20:2000;2367-2377.
30. Schwienhorst I., et al. SUMO conjugation and deconjugation. Mol. Gen. Genet. 263:2000;771-786.
31. Panse V.G., et al. Unconventional tethering of Ulp1 to the transport channel of the nuclear pore complex by karyopherins. Nat. Cell Biol. 5:2003;21-27.
32. Bachant J., et al. The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II. Mol. Cell. 9:2002;1169-1182.
33. Mendoza H.M., et al. NEDP1, a highly conserved cysteine protease that deNEDDylates cullins. J. Biol. Chem. 278:2003;25637-25643.
34. Gan-Erdene T., et al. Identification and characterization of DEN1, a deneddylase of the ULP family. J. Biol. Chem. 278:2003;28892-28900.
35. Wu K., et al. DEN1 is a dual function protease capable of processing the C-terminus of Nedd8 deconjugating hyper-neddylated CUL1. J. Biol. Chem. 278:2003;28882-28891.
36. Kim K.I., et al. A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs. J. Biol. Chem. 275:2000;14102-14106.
37. Nishida T., et al. A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the nucleolus at interphase. Eur. J. Biochem. 267:2000;6423-6427.
38. Nishida T., et al. Characterization of a novel mammalian SUMO-1/Smt3-specific isopeptidase, a homologue of rat Axam, which is an Axin-binding protein promoting β-catenin degradation. J. Biol. Chem. 276:2001;39060-39066.
39. Gong L., et al. Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J. Biol. Chem. 275:2000;3355-3359.
40. Zhang H., et al. Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex. Mol. Cell. Biol. 22:2002;6498-6508.
41. Kadoya T., et al. Desumoylation activity of Axam, a novel Axin-binding protein, is involved in downregulation of β-catenin. Mol. Cell. Biol. 22:2002;3803-3819.
42. Bailey D., O'Hare P. Herpes simplex virus 1 ICP0 co-localizes with a SUMO-specific protease. J. Gen. Virol. 83:2002;2951-2964.
43. Hang J., Dasso M. Association of the human SUMO-1 protease SENP2 with the nuclear pore. J. Biol. Chem. 277:2002;19961-19966.
44. Best J.L., et al. SUMO-1 protease-1 regulates gene transcription through PML. Mol. Cell. 10:2002;843-855.
45. Muller S., et al. c-Jun and p53 activity is modulated by SUMO-1 modification. J. Biol. Chem. 275:2000;13321-13329.
46. Yang S.H., et al. Dynamic interplay of the SUMO and ERK pathways in regulating Elk-1 transcriptional activity. Mol. Cell. 12:2003;63-74.
47. Hietakangas V., et al. Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1. Mol. Cell. Biol. 23:2003;2953-2968.
48. Hilgarth R.S., et al. Insights into the regulation of heat shock transcription factor 1 SUMO-1 modification. Biochem. Biophys. Res. Commun. 303:2003;196-200.
49. Taylor D.L., et al. Cell-cycle-dependent localisation of Ulp1, a Schizosaccharomyces pombe Pmt3 (SUMO)-specific protease. J. Cell Sci. 115:2002;1113-1122.
50. Takahashi Y., et al. Yeast Ulp1, an Smt3-specific protease, associates with nucleoporins. J. Biochem. (Tokyo). 128:2000;723-725.
51. Weis K. Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell. 112:2003;441-451.
52. Wood L.D., et al. Small ubiquitin-like modifier conjugation regulates nuclear export of TEL, a putative tumor suppressor. Proc. Natl. Acad. Sci. U. S. A. 100:2003;3257-3262.
53. Stade K., et al. A lack of SUMO conjugation affects cNLS-dependent nuclear protein import in yeast. J. Biol. Chem. 277:2002;49554-49561.
54. Kahyo T., et al. Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol. Cell. 8:2001;713-718.
55. Nishida T., Yasuda H. PIAS1 and PIASxα function as SUMO-E3 ligases toward androgen receptor and repress androgen receptor-dependent transcription. J. Biol. Chem. 277:2002;41311-41317.
56. Kotaja N., et al. PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases. Mol. Cell. Biol. 22:2002;5222-5234.
57. Sapetschnig A., et al. Transcription factor Sp3 is silenced through SUMO modification by PIAS1. EMBO J. 21:2002;5206-5215.
58. Nakagawa K., Yokosawa H. PIAS3 induces SUMO-1 modification and transcriptional repression of IRF-1. FEBS Lett. 530:2002;204-208.
59. Rogers R.S., et al. SUMO modification of STAT1 and its role in PIAS-mediated inhibition of gene activation. J. Biol. Chem. 278:2003;30091- 30097.
60. Sachdev S., et al. PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. Genes Dev. 15:2001;3088-3103.
61. Yamamoto H., et al. Sumoylation is involved in β-catenin-dependent activation of Tcf-4. EMBO J. 22:2003;2047-2059.
62. Dahle O., et al. Transactivation properties of c-Myb are critically dependent on two SUMO-1 acceptor sites that are conjugated in a PIASy enhanced manner. Eur. J. Biochem. 270:2003;1338-1348.
63. Subramanian L., et al. A synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein α inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3. J. Biol. Chem. 278:2003;9134-9141.
64. Kirsh O., et al. The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. EMBO J. 21:2002;2682-2691.