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Versatile protein tag, SUMO: its enzymology and biological function

Authors
김근일Sung Hee BaekChin 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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