Abstract
Ubiquitylation describes a process in which ubiquitin, a 76-amino-acid polypeptide, is covalently attached to target proteins. Traditionally, ubiquitin-conjugated proteins are targeted for degradation by the 26S proteasome. However, non-proteolytic roles in histone regulation, DNA repair and signal transduction have been reported. Here, the role of ubiquitylation in the cell death pathway in Drosophila is reviewed. Interestingly, ubiquitylation serves both pro- and anti-apoptotic functions. Although pro-apoptotic ubiquitylation leads to proteolytic degradation, recent evidence suggests that anti-apoptotic ubiquitylation may involve, at least in part, non-proteolytic functions.
