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Background
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Covalent modification of target lysines by SUMO (small ubiquitin-like modifier) modulates processes such as protein localization, transcription, nuclear transport, mitosis, DNA replication and repair, signal transduction, and viral reproduction. SUMO does not seem to be involved in protein degradation and may in fact function as an antagonist of ubiquitin in the degradation process. The SUMO family consists of SUMO1 and closely related homologs SUMO2, SUMO3, and SUMO4. Sumoylation has been shown to regulate a wide range of proteins, including MDM2, PIAS, PML, RanGAP1, RanBP2, p53, p73, HIPK2, TEL, c-Jun, Fas, Daxx, TNFRI, Topo-I, Topo-II, PARK2, WRN, Sp100, IkB-alpha, Androgen receptor (AR), GLUT1/4, CaMK, DNMT3B, TDG, HIF1A, CHD3, EXOSC9, RAD51, and viral targets such as CMV-IE1/2, EBV-BZLF1, and HPV/BPV-E1.
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Background
References
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- Yang, S.H., et al., Mol. Cell 13(4):611-617 (2004).
- Bailey, D., et al., J. Biol. Chem. 279(1):692-703 (2004).
- Ling, Y., et al., Nucleic Acids Res. 32(2):598-610 (2004).
- Pountney, D.L., et al., Exp. Neurol. 184(1):436-446 (2003).
- Ohshima, T., et al., J. Biol. Chem. 278(51):50833-50842 (2003).
- Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).
- Lapenta, V., et al., Genomics 40(2):362-366 (1997).
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