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Cell Death Differ. 2010 Jan;17(1):61-7. doi: 10.1038/cdd.2009.70.

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

Author information

1
Department of Biochemistry and Molecular Biology, Graduate Program in Genes and Development, The University of Texas M.D. Anderson Cancer Center, Houston, TX 77030, USA. abergman@mdanderson.org

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.

PMID:
19498442
PMCID:
PMC2813689
DOI:
10.1038/cdd.2009.70
[Indexed for MEDLINE]
Free PMC Article

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