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SUMOylation in Drosophila Development
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
These authors contributed equally to this work.
* Author to whom correspondence should be addressed.
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 conjugation pathway regulates a wide variety of critical cellular and developmental processes, including chromatin/chromosome function, eggshell patterning, embryonic pattern formation, metamorphosis, larval and pupal development, neurogenesis, development of the innate immune system, and apoptosis. This review discusses our current understanding of the diverse roles for SUMO in Drosophila development.
Keywords: SUMO; Ubc9; chromatin; pattern formation; wing morphogenesis; Ras signaling; metamorphosis; innate immunity
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MDPI and ACS Style
Smith, M.; Turki-Judeh, W.; Courey, A.J. SUMOylation in Drosophila Development. Biomolecules 2012, 2, 331-349.
Smith M, Turki-Judeh W, Courey AJ. SUMOylation in Drosophila Development. Biomolecules. 2012; 2(3):331-349.
Smith, Matthew; Turki-Judeh, Wiam; Courey, Albert J. 2012. "SUMOylation in Drosophila Development." Biomolecules 2, no. 3: 331-349.