SUMOylation in Drosophila Development

Biomolecules

Matthew Smith¹  Wiam Turki-Judeh¹ 

关键词: SUMO;    Ubc9;    chromatin;    pattern formation;    wing morphogenesis;    Ras signaling;    metamorphosis;    innate immunity;   

DOI  :  10.3390/biom2030331

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2012 by the authors; licensee MDPI, Basel, Switzerland.