SUMO4

Sub-Areas to SUMO4:

Polymorphism (7)


(Journal Article): Is a New Immune Response Mediator in the NF-κB pathway - SUMO-4 - Related to Type 1 Diabetes?
 
Sia C (Department of Immunology, United Biomedical Inc., 25 Davids Drive, Hauppage, New York 11788, USA., csia(at)unitedbiomedical.com )
 
IN: Rev Diabetic Stud 2005; 2(2):58-60
Impact Factor(s) of Rev Diabetic Stud: 0.125 (2006)

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ABSTRACT: Type 1 diabetes mellitus (T1DM) is hallmarked by a complete loss of insulin secretion capacity caused by T cell-mediated destruction of pancreatic β-cells [1, 2]. The disorder has a complex pathogenesis involving genetic and environmental factors, it appears impossible hitherto to explain sufficiently how islet abnormalities arise and which mechanisms trigger immune cells to become diabetogenic.

TYPE OF PUBLICATION: Review

REFERENCES:

  1. Kay TW, Thomas HE, Harrison LC, Allison J. The beta cell in autoimmune diabetes: many mechanisms and pathways of loss. Trends Endocrinol Metab 2000. 11(1):11-15. [DOD]
  2. Kurrer MO, Pakala SV, Hanson HL, Katz JD. Beta cell apoptosis in T cell-mediated autoimmune diabetes. Proc Natl Acad Sci U S A 1997. 94(1):213-218. [DOD]
  3. Daniel D, Gill RG, Schloot N, Wegmann D. Epitope speci-ficity, cytokine production profile and diabetogenic activity of insulin-specific T cell clones isolated from NOD mice. Eur J Immunol 1995. 25(4):1056-1062. [DOD]
  4. Rabinovitch A. An update on cytokines in the pathogenesis of insulin-dependent diabetes mellitus. Diabetes Metab Rev 1998. 14:129-151. [DOD]
  5. Ghosh S, May MJ, Kopp EB. NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 1998. 16:225-260. [DOD]
  6. Cardozo AK, Heimberg H, Heremans Y, Leeman R, Kutlu B, Kruhoffer M, Orntoft T, Eizirik DL. A compre-hensive analysis of cytokine-induced and nuclear factor-kappa B-dependent genes in primary rat pancreatic beta-cells. J Biol Chem 2001. 276(52):48879-48886. [DOD]
  7. Hayashi T, Faustman D. NOD mice are defective in protea-some production and activation of NF-kappaB. Mol Cell Biol 1999. 19(12):8646-8659. [DOD]
  8. Eizirik DL, Mandrup-Poulsen T. A choice of death - the signal-transduction of immune-mediated beta-cell apoptosis. Diabetologia 2001. 44(12):2115-2133. [DOD]
  9. Gylvin T, Bergholdt R, Nerup J, Pociot F. Characterization of a nuclear-factor-kappa B (NFkappaB) genetic marker in type 1 diabetes (T1DM) families. Genes Immun 2002. 3(7):430-432. [DOD]
  10. Hegazy DM, O'Reilly DA, Yang BM, Hodgkinson AD, Millward BA, Demaine AG. NFkappaB polymorphisms and susceptibility to type 1 diabetes. Genes Immun 2001. 2(6):304-308. [DOD]
  11. Lgssiar A, Hassan M, Schott-Ohly P, Friesen N, Nicoletti F, Trepicchio WL, Gleichmann H. Interleukin-11 inhibits NF-kappaB and AP-1 activation in islets and prevents diabetes induced with streptozotocin in mice. Exp Biol Med (Maywood) 2004. 229(5):425-436. [DOD]
  12. Mabley JG, Hasko G, Liaudet L, Soriano F, Southan GJ, Salzman AL, Szabo C. NFkappaB1 (p50)-deficient mice are not susceptible to multiple low-dose streptozotocin-induced diabetes. J Endocrinol 2002. 173(3):457-464. [DOD]
  13. Matunis MJ, Pickart CM. Beginning at the end with SUMO. Nat Struct Mol Biol 2005. 12(7):565-566. [DOD]
  14. Seeler JS, Dejean A. Nuclear and unclear functions of SU-MO. Nat Rev Mol Cell Biol 2003. 4(9):690-699. [DOD]
  15. Muller S, et al. SUMO: a regulator of gene expression and genome integrity. Oncogene 2004. 23(11):1998-2008. [DOD]
  16. Guo D, Li M, Zhang Y, Yang P, Eckenrode S, Hopkins D, Zheng W, Purohit S, Podolsky RH, Muir A, et al. A functional variant of SUMO4, a new I kappa B alpha modifier, is associated with type 1 diabetes. Nat Genet 2004. 36(8):837-841. [DOD]
  17. Li M, Guo D, Isales CM, Eizirik DL, Atkinson M, She JX, Wang CY. SUMO wrestling with type 1 diabetes. J Mol Med 2005. 83(7):504-513. [DOD]
  18. Kosoy R, Concannon P. Functional variants in SUMO4, TAB2, and NFkappaB and the risk of type 1 diabetes. Genes Immun 2005. 6(3):231-235. [DOD]
  19. Bohren KM, Nadkarni V, Song JH, Gabbay KH, Owerbach D. A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription fac-tors and is associated with susceptibility to type I diabetes mel-litus. J Biol Chem 2004. 279(26):27233-27238. [DOD]
  20. He H, Soncin F, Grammatikakis N, Li Y, Siganou A, Gong J, Brown SA, Kingston RE, Calderwood SK. Ele-vated expression of heat shock factor (HSF) 2A stimulates HSF1-induced transcription during stress. J Biol Chem 2003. 278(37):35465-35475. [DOD]
  21. Alastalo TP, Hellesuo M, Sandqvist A, Hietakangas V, Kallio M, Sistonen L. Formation of nuclear stress granules involves HSF2 and coincides with the nucleolar localization of Hsp70. J Cell Sci 2003. 116:3557-3570. [DOD]
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  23. Qu H, Bharaj B, Liu XQ, Curtis JA, Newhook LA, Paterson AD, Hudson TJ, Polychronakos C. Assessing the validity of the association between the SUMO4 M55V variant and risk of type 1 diabetes. Nat Genet 2005. 37(2):111-112. [DOD]
  24. Park Y, Park S, Kang J, et al. Additional support for a ge-netic association between SUMO4 and type 1 diabetes in the Korean population. Nat Genet (in press). [DOD]
  25. Wang CY, Yang P, She JX. Genetic heterogeneity of the IDDM5 (SUMO4) locus. Nat Genet (in press). [DOD]

 
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(Journal Article): Beginning at the end with SUMO.
 
Matunis MJ, Pickart CM (Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland 21205, USA., cpickart@jhmi.edu )
 
IN: Nat Struct Mol Biol 2005; 12(7):565-566
Impact Factor(s) of Nat Struct Mol Biol: 12.0 (2004)

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ABSTRACT: The crystal structure of a four-protein complex comprising a SUMO ligase (E3), a SUMOylated protein substrate, and the cognate SUMO-conjugating enzyme sheds new light on catalysis, specificity and SUMO-protein interactions.

TYPE OF PUBLICATION: Original article

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(Journal Article): Nuclear and unclear functions of SUMO.
 
Seeler JS, Dejean A (Nuclear Organization and Oncogenesis Unit, INSERM U 579, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France.)
 
IN: Nat Rev Mol Cell Biol 2003; 4(9):690-699
Impact Factor(s) of Nat Rev Mol Cell Biol: 29.852 (2005), 33.17 (2004), 35.041 (2003), 20.556 (2001)

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ABSTRACT: Post-translational modification by the ubiquitin-like SUMO protein is emerging as a defining feature of eukaryotic cells. Sumoylation has crucial roles in the regulatory challenges that face nucleate cells, including the control of nucleocytoplasmic signalling and transport and the faithful replication of a large and complex genome, as well as the regulation of gene expression.

TYPE OF PUBLICATION: Original article

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(Journal Article): SUMO: a regulator of gene expression and genome integrity.
 
Muller S, Ledl A, Schmidt D (Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany., stmuelle@biochem.mpg.de )
 
IN: Oncogene 2004; 23(11):1998-2008
Impact Factor(s) of Oncogene: 6.318 (2004), 6.495 (2003), 5.979 (2002), 6.737 (2001)

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ABSTRACT: Post-translational modification with the ubiquitin-like SUMO protein is involved in the regulation of many cellular key processes. The SUMO system modulates signal transduction pathways, including cytokine, Wnt, growth factor and steroid hormone signalling. SUMO frequently restrains the activity of downstream transcription factors in these pathways presumably by facilitating the recruitment of corepressors or mediating the assembly of repressor complexes. Additionally, evidence is accumulating that SUMO controls pathways important for the surveillance of genome integrity. SUMO regulates the PML/p53 tumour suppressor network, a key determinant in the cellular response to DNA damage. Moreover, proteins that maintain genomic stability by functioning at the interface between DNA replication, recombination and repair processes undergo SUMOylation. We will discuss some key findings that exemplify the role of SUMO in transcriptional regulation and genome surveillance.

TYPE OF PUBLICATION: Original article

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