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.
Highlights
Small ubiquitin-related modifier (SUMO), an ~90 amino acid ubiquitin-like protein, is highly conserved throughout the eukaryotic domain
SUMO family proteins [2,3], the Drosophila genome encodes one such protein [4] which is more similar to human SUMO-2/3/4 than it is to human SUMO-1
Maturation of SUMO is accomplished by the activity of a ubiquitin-like protease (Ulp), which removes a C-terminal extension from the immature protein exposing a Gly-Gly motif at the C-terminus
Summary
Small ubiquitin-related modifier (SUMO) is a Ubiquitin-Like protein (UbL). SUMO becomes covalently attached to lysine side chains in a variety of target proteins in a process termed SUMOylation. It is synthesized as an inactive precursor that must undergo maturation before it can proceed through the enzymatic steps required for conjugation to target proteins. Maturation of SUMO is accomplished by the activity of a ubiquitin-like protease (Ulp), which removes a C-terminal extension from the immature protein exposing a Gly-Gly motif at the C-terminus. This thioester linkage is transferred to an active site cysteine within the conjugating enzyme Ubc (which is encoded by the Drosophila gene lesswright (lwr)) [6]. It is primarily associated with the nucleoplasmic face of the nuclear pore complex where it may deconjugate proteins as they exit the nucleus serving as a molecular switch to control the biochemical properties of a protein as a function of its subcellular location
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