Versatile protein tag, SUMO: its enzymology and biological function
- Authors
- 김근일; Sung Hee Baek; Chin Ha Chung
- Issue Date
- Apr-2002
- Publisher
- Wiley InterScience
- Keywords
- UBIQUITIN-LIKE PROTEIN; NF-KAPPA-B; ACUTE PROMYELOCYTIC LEUKEMIA; GTPASE-ACTIVATING PROTEIN; TUMOR-SUPPRESSOR P53; NUCLEAR-PORE COMPLEX; MEDIATED TRANSCRIPTIONAL REPRESSION; AXIN-BINDING PROTEIN; PML-RAR-ALPHA; COVALENT MODIFICATION
- Citation
- Journal of Cellular Physiology, v.191, no.3, pp 257 - 268
- Pages
- 12
- Journal Title
- Journal of Cellular Physiology
- Volume
- 191
- Number
- 3
- Start Page
- 257
- End Page
- 268
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/149331
- DOI
- 10.1002/jcp.10100
- ISSN
- 0021-9541
1097-4652
- Abstract
- Small ubiquitin-related modifier (SUMO) is a member of a ubiquitin-like protein family that regulates cellular function of a variety of target proteins. SUMO and ubiquitin are synthesized as precursors that need to be processed prior to conjugation to target proteins, and their mature forms have a similar tertiary structure. The mechanism for SUMO conjugation is also analogous to that of the ubiquitin system, such as the utilization of E1, E2, and E3 cascade enzymes. However, the biological consequence of SUMO modification is quite different from that of the ubiquitin system. Whereas ubiquitination of most proteins is for the degradative pathway, SUMO modification of target proteins is involved in nuclear protein targeting, formation of subnuclear structures, regulation of transcriptional activities or DNA binding abilities of transcription factors, and control of protein stability. This review will summarize the recent progress made in the enzymology of SUMO and its biological significance. (C) 2002 Wiley-Liss, Inc.
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