The role of ubiquitylation for the control of cell death in Drosophila

• Published in: Cell death and differentiation Vol. 17; no. 1; pp. 61 - 67
• Main Author: Bergmann, A
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 01-01-2010; Nature Publishing Group
• Subjects: Animals; Apoptosis; Biochemistry; Biomedical and Life Sciences; Caspases - metabolism; Cell Biology; Cell Cycle Analysis; Cell death; Drosophila; Drosophila - genetics; Drosophila - metabolism; Drosophila Proteins - metabolism; Inhibitor of Apoptosis Proteins - metabolism; Ion Channels; Life Sciences; review; Stem Cells; TRPA1 Cation Channel; TRPC Cation Channels - metabolism; Ubiquitin - metabolism; Ubiquitination - physiology; apoptosis; IAP; cell death; ubiquitin
• ISSN: 1350-9047; 1476-5403
• DOI: 10.1038/cdd.2009.70

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 26
S
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.