sumoylation in drosophila developmentsumoylation果蝇发展.pdfVIP

Biomolecules 2012, 2, 331-349; doi:10.3390/biom2030331 OPEN ACCESS biomolecules ISSN 2218-273X /journal/biomolecules/ Review SUMOylation in Drosophila Development Matthew Smith †, Wiam Turki-Judeh † and Albert J. Courey * Department of Chemistry Biochemistry and Molecular Biology Institute, University of California-Los Angeles, 607 Charles E. Young Drive East, Los Angeles, CA 90095-1569, USA; E-Mails: msmith@ (M.S.); wiamtj@ (W.T.-J.) † These authors contributed equally to this work. * Author to whom correspondence should be addressed; E-Mail: courey@; Tel.: +1-310-825-2530; Fax: +1-310-206-4038. Received: 13 June 2012; in revised form: 23 June 2012 / Accepted: 25 June 2012 / Published: 25 July 2012 Abstract: Small ubiquitin-related modifier (SUMO), an ~90 amino acid ubiquitin-like protein, is highly conserved throughout the eukaryotic domain. Like ubiquitin, SUMO is covalently attached to lysine side chains in a large number of target proteins. In contrast to ubiquitin, SUMO does not have a direct role in targeting proteins for proteasomal degradation. However, like ubiquitin, SUMO does modulate protein function in a variety of other ways. This includes effects on protein conformation, subcellular localization, and protein–protein interactions. Significant insight into the in vivo role of SUMOylation has been provided by studies in Drosophila that combine genetic manipulation, proteomic, and biochemical analysis. Such studies have revealed that the SUMO conjugatio