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Biomolecules 2012, 2(3), 331-349; doi:10.3390/biom2030331
Review

SUMOylation in Drosophila Development

,
 and *
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 / Revised: 23 June 2012 / Accepted: 25 June 2012 / Published: 25 July 2012
(This article belongs to the Special Issue Protein SUMOylation)
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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 SUMO; Ubc9; chromatin; pattern formation; wing morphogenesis; Ras signaling; metamorphosis; innate immunity
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Smith, M.; Turki-Judeh, W.; Courey, A.J. SUMOylation in Drosophila Development. Biomolecules 2012, 2, 331-349.

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