Ubiquitins, proteasomes, sumoylation and application today and in future for cancer and other diseases therapy II. Sumoylation and neddylation as posttranslational modifications of proteins and their significance;Ubikvitiny, proteazomy, sumoylace a použití dnes a zítra v terapii nádorů i jiných chorob II. Sumoylace a neddylace jako posttranslační modifikace proteinů podobné ubikvitinylaci a jejich význam

Vnitrni Lekarstvi

Volumn 52, Issue 6, 2006, Pages 619-627

  Fuchs, Ota ^a   Neuwirtova R ^b  

^a INSTITUTE OF HEMATOLOGY AND BLOOD TRANSFUSION   (Czech Republic)

^b CHARLES UNIVERSITY   (Czech Republic)

Author keywords

Nedd8; Neddylation; SUMO; Sumoylation; Ubiquitin like protein modifiers

Indexed keywords

NEDD8 PROTEIN; PROTEASOME; SUMO PROTEIN; UBIQUITIN; NEDD8 PROTEIN, HUMAN; SUMO 1 PROTEIN;

CANCER; CELL DIFFERENTIATION; CYTOPLASM; DNA REPAIR; PROTEIN BINDING; PROTEIN DEGRADATION; REVIEW; SIGNAL TRANSDUCTION; UBIQUITINATION; HUMAN; METABOLISM; NEOPLASM; PROTEIN PROCESSING;

HUMANS; NEOPLASMS; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEIN PROCESSING, POST-TRANSLATIONAL; SUMO-1 PROTEIN; UBIQUITINS;

EID: 33745745132     PISSN: 0042773X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (77)

1. Matunis MJ, Coutavas E, Blobel G. 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 1996; 135: 1457-1470.
2. Mahajan R, Delphin C, Guan T et al. A small-ubiquitin related polypeptide involved in targeting Ran-GAP1 to nuclear pore complex protein RanBP2. Cell 1997; 88: 97-107.
3. Boddy MN, Howe K, Etkin LD et al. PIC1, a novel ubiquitin-like protein which interacts with the PML component of multiprotein complex that is disrupted in acute promyelocytic leukaemia, Oncogene 1996; 13: 971-982.
4. Okura T, Gong L, Kamitani T et al. Protection against Fas/APO-1 and tumor necrosis factor-mediated cell death by a novel protein, sentrin. J Immunol 1966; 157: 4277-4281.
5. Mannen H, Tseng HM, Cho CL et al. Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene. Biochem Biophys Res Commun 1966; 222: 178-180.
6. Shen Z, Pardington-Purtymun PE, Comeaux JC et al. UBL1, a human ubiquitin-like protein associating with human RAD51/RAD52 proteins. Genomics 1966; 36: 271-279.
7. Dohmen RJ. SUMO protein modification. Biochim Biophys Acta 2004; 1695: 113-131.
8. Hilgarth RS, Murphy LA, Skaggs HS et al. Regulation and function of SUMO modification. J Biol Chem 2004; 279: 53899-53902.
9. Kumar S, Yoshida Y, Noda M. Cloning of a cDNA which encodes a novel ubiquitin-like protein. Biochem Biophys Res Commun 1993; 195: 393-399.
10. Kamitani T, Kito K, Nguyen HP et al. Characterization of NEDD8, a developmentally down-regulated ubiquitin-like protein. J Biol Chem 1997; 272: 28557-28562.
11. Saitoh H, Hinchey J. Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J Biol Chem 2000; 275: 6252-6258.
12. Dohmen RJ. SUMO protein modification. Biochim Biophys Acta 2004; 1695: 113-131.
13. Azuma Y, Arnaoutov A, Dasso M. SUMO-2/3 regulates topoisomerase II in mitosis. J Cell Biol 2003; 163: 477-487.
14. Bohren KM, Nadkarni V, Song JH et al. 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 2004; 279: 27233-27238.
15. Guo D, Li M, Zhang Y et al. A functional variant of SUMO-4, a new IκBα moldifier, is associated with type 1 diabetes. Nat Genet 2004; 36: 837-841.
16. Owerbach D, Pina L, Gabbay KH. A 212-kb region on chromosome 6q25 containing TAB2 gene is associated with susceptibility to type 1 diabetes. Diabetes 2004; 53: 1890-1893.
17. Li M, Guo D, Isales CM et al. SUMO wrestling with type 1 diabetes. J Mol Med 2005; 83: 504-513.
18. Johnson ES. Protein modification by SUMO. Annu Rev Biochem 2004; 73: 355-382.
19. Schwartz DC, Hochstrasser M. A superfamily of protein tags: ubiquitin, SUMO and related modifiers. Trends Biochem Sci 2003; 28: 321-328.
20. Gill G. SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? Genes Dev 2004; 18: 2046-2059.
21. Hay RT. SUMO: a history of modification. Mol Cell 2005; 18: 1-12.
22. Melchior F, Schergaut M., Pichler A. SUMO: ligases, isopeptidases and nuclear pores. Trends Biochem Sci 2003; 28: 612-616.
23. Desterro JM, Thomson J, Hay RT. Ubch9 conjugates SUMO but not ubiquitin. FEBS Lett 1997; 417: 297-300.
24. Kahyo T, Nishida T, Yasuda H. Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol Cell 2001; 8: 713-718.
25. Sachdev S, Bruhn L, Sieber H et al. PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. Genes Dev 2001; 15: 3088-3103.
26. Pichler A, Gast A, Seeler JS et al. The nucleoporin Ran BP2 has SUMO1 E3 ligase activity. Cell 2002; 108: 109-120.
27. Pichler A, Knipscheer P, Saitoh H et al. The Ran-BP2 SUMO E3 ligase is neither HECT- nor RING- type. Nat Struct Mol Biol 2004; 11: 984-991.
28. Kagey MH, Melhuish TA, Powers SE et al. Multiple activities contribute to Pc2 E3 function. EMBO J 2005; 24: 108-119.
29. Verger A, Perdomo J, Crossley M. Modification with SUMO. A role in transcriptional regulation. EMBO Rep 2003; 48: 137-142.
30. Hay RT. Protein modification by SUMO. Trends Biochem Sci 2001; 26: 332-333.
31. Kim KI, Baek SH, Chung CH. Versatile protein tag, SUMO: its enzymology and biological function. J Cell Physiol 2002; 191: 257-268.
32. Xu Z, Au SWN. Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1. Biochem J 2005; 386: 325-330.
33. Stewart M. Nuclear trafficking. Science 2003; 302: 1513-1514.
34. Fahrenkrog B, Köser J, Aebi U. The nuclear pore complex: a jack of all trades? Trends Biochem Sci 2004; 29: 175-182.
35. Lee SJ, Matsuura Y, Man Liu S et al. Structural basis for nuclear import complex dissociation by RanGTP. Nature 2005; 435: 693-696.
36. + channel K2p1. Cell 2005; 121: 37-47.
37. Gill G. Post-translational modification by the small ubiquitin-related modifier SUMO has big effects on transcription factor activity. Curr Opin Genet Dev 2003; 13: 108-113.
38. Verger A, Perdomo J, Crossley M. Modification with SUMO. A role in transcriptional regulation. EMBO Rep 2003; 48: 137-142.
39. Gill G. Something about SUMO inhibits transcription. Curr Opin Genet Dev 2005; 15: 1-6.
40. Hilgarth RS, Murphy LA, Skaggs HS et al. Regulation and function of SUMO modification. J Biol Chem 2004; 279: 53899-53902.
41. Yamamoto H, Ihara M, Matsuura Y et al. Sumoylation is involved in β-catenin-dependent activation of Tcf-4. EMBO J 2003; 22: 2047-2059.
42. Gomez-del Arco P, Koipally J, Georgopoulos K. Ikaros SUMOylation: switching out of repression. Mol Cell Biol 2005; 25: 2688-2697.
43. Girdwood D, Bumpass D, Vaughan OA et al. P300 transcriptional repression is mediated by SUMO modification. Mol Cell 2003; 11: 1043-1054.
44. David G, Neptune MA, DePinho RA. SUMO-1 modification of histone deacetylase 1 (HDAC 1) modulates its biological activities. J Biol Chem 2002; 277: 23658-23663.
45. Zhang Y. Transcriptional regulation by histone ubiquitination and deubiquitination. Genes Dev 2003; 17: 2733-2740.
46. Nathan D, Sterner DE, Berger SL. Histone modifications: Now summoning sumoylation. Proc Natl Acad Sci USA 2003; 100: 13118-13120.
47. Shiio Y, Eisenman RN. Histone sumoylation is associated with transcriptional repression. Proc Natl Acad Sci USA 2003; 100: 13225-13230.
48. Hoege C, Pfander B, Moldavan GL et al. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 2002; 419: 135-141.
49. Stelter P, Ulrich HD. Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature 2003; 425: 188-191.
50. Papouli E, Chen S, Davies AA et al. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol Cell 2005; 19: 123-133.
51. Nevels M, Brune W, Shenk T. Sumoylation of the human cytomegalovirus 72-kilodalton IE1 protein facilitates expression of the 86-kilodalton IE2 protein and promotes viral replication. J Virol 2004; 78: 7803-7812.
52. Gravel A, Don V, Cloutier N et al. Characterization of human herpesvirus 6 variant B immediate-early 1 protein modifications by small ubiquitin-related modifiers. J Gen Virol 2004; 85: 1319-1328.
53. Gurer C, Berthoux L, Luban J. Covalent modification of human immunodeficiency virus type 1 p6 by SUMO-1. J Virol 2005; 79: 910-917.
54. Glotzer JB, Saltik M, Chiocca S et al. Activation of heat-shock response by an adenovirus is essential for virus replication. Nature 2000; 407: 207-211.
55. Colombo R, Boggio R, Seiser C et al. The adenovirus protein Gam1 interferes with sumoylation of histone deacetylase 1. EMBO Rep 2002; 3: 1062-1068.
56. Boggio R, Colombo R, Hay RT et al. A mechanism for inhibiting the SUMO pathway. Mol Cell 2004; 16: 549-561.
57. Steffan JS, Agrawal N, Pallos J et al. SUMO modification of Huntingtin and Huntington's disease pathology. Science 2004; 304: 100-104.
58. Ueda H, Goto J, Hashida J et al. Enhanced SUMOylation in polyglutamine diseases. Biochem Biophys Res Commun 2002; 293: 307-313.
59. Chan HY, Warrick JM, Andriola I et al. Genetic modulation of polyglutamine toxicity by protein conjugation pathways in Drosophila. Hum Mol Genet 2002; 11: 2895-2904.
60. Poutney DL, Huang Y, Burns RJ et al. SUMO-1 marks the nuclear inclusions in familial neuronal intranuclear inclusion disease. Exp Neurol 2003; 184: 436-446.
61. Li Z, Wang H, Wang S et al. Positive and negative regulation of APP amyloidogenesis by sumoylation. Proc Natl Acad Sci USA 2003; 100: 259-264.
62. Kamitani T, Kito K, Nguyen HP et al. Identification of three major sentinization sites in PML. J Biol Chem 1998; 273: 26675-26682.
63. Duprez E, Saurin AJ, Desterro JM et al. SUMO-1 modification of the acute promyelocytic leukaemia protein PML: implications for nuclear localisation. J Cell Sci 1999; 112: 381-393.
64. Zhong S, Muller S, Ronchetti S et al. Role of SUMO-1 modified PML in nuclear body formation. Blood 2000; 95: 2748-2753.
65. Müller S, Matunis MJ, Dejean A. Conjugation with the ubiquitin-related modifier SUMO-1 regulates the partitioning of PML within the nucleus. EMBO J 1998; 17: 61-70.
66. Osaka F, Kawasaki H, Aida N et al. A new NEDD8-ligating system for cullin 4A. Genes Dev 1998; 12: 2263-2268.
67. Morimoto M, Nishida T, Nagayama Y et al. Nedd8- modification of Cull is promoted by Roc1 as a Nedd8-E3 ligase and regulates its stability. Biochem Biophys Res Commun 2003; 301: 392-398.
68. Pan ZQ, Kentis A, Dias DC et al. Nedd8 on cullin: building an expressway to protein destruction. Oncogene 2004; 23: 1985-1997.
69. Regulation of cullin-based ubiquitin ligases by the Nedd8/RUB ubiquitin-like proteins. Semin Cell Dev Biol 2004; 15: 221-229.
70. Wei N, Deng XW. The COP9 signalosome. Annu Rev Cell Dev Biol 2003; 19: 261-286.
71. Schwechheimer C. The COP9 signalosome (CSN): an evolutionary conserved proteolysis regulator in eukaryotic development. Biochim Biophys Acta 2004; 1695: 45-54.
72. Min KW, Kwon MJ, Park HS et al. CAND1 enhances deneddylation of CUL1 by COP9 signalosome. Biochem Biopys Res Commun 2005; 334: 867-874.
73. Ohh M, Kim WZ, Moslehi JJ et al. An intact NEDD8 pathway is required for cullin-dependent ubiquitylation in mammalian cells. EMBO Rep 2002; 3: 177-182.
74. Guardavaccoro D, Pagano M. Oncogenic aberrations of cullin-dependent ubiquitin ligases. Oncogene 2004; 23: 2037-2049.
75. Ang XL, Harper JW. SCF-mediated protein degradation and cell cycle control. Oncogene 2005; 24: 2860-2870.
76. Busino L, Chiesa M, Draetta GF et al. Cdc25A phosphatase: combinatorial phosphorylation, ubiquitylation and proteolysis. Oncogene 2004; 23: 2050-2056.
77. Fuchs O, Neuwirtová R. Ubikvitiny, proteazomy, sumoylace a použití dnes a zítra v terapii nádorů i jiných chorob I. Ubikvitin-proteazomový systém a transkripční faktor NF-κB. Vnitř Lék 2006; 52(4): 371-378.