IAPS and ubiquitylation
Author(s)
Feltham, R; Khan, N; Silke, J;
Details
Publication Year 2012-05, Volume 64, Issue #5, Page 411-418
Journal Title
IUBMB LIFE
Publication Type
Journal Article
Abstract
The Inhibitor of apoptosis (IAP) proteins are key negative regulators of cell death, whose amplification has been correlated with tumor progression. Due to the presence of a RING domain, IAP proteins are classed as ubiquitin ligases and regulate cell survival by orchestrating a variety of ubiquitin modifications. Ubiquitin protein modification is fundamental in cell signaling and different ubiquitin modifications may label proteins for destruction, relocalization or provide a recruitment platform for ubiquitin binding proteins. Ubiquitin performs a myriad of different functions because it can be conjugated to a large range of target proteins through numerous different types of ubiquitin linkages. Despite the fact that ubiquitin is extremely versatile, the E3s such as the IAPs provide an important level of control due to their specificity for certain substrates. Several recent reviews have discussed the role of IAPs in regulating immune signaling so we have therefore focused our review on the interplay between IAPs and ubiquitin and discussed the importance of this relationship for the regulation of themselves, specific substrates and various cell death and survival signaling pathways. (c) 2012 IUBMB Life, 2012
Publisher
WILEY-BLACKWELL
Keywords
IAPs ; ubiquitin ligases ; apoptosis ; necrosis
WEHI Research Division(s)
Cell Signalling And Cell Death
Publisher's Version
https://doi.org/10.1002/iub.565
Rights Notice
Copyright © 2012 Wiley Periodicals, Inc.


Creation Date: 2012-05-01 12:00:00
Last Modified: 0001-01-01 12:00:00
An error has occurred. This application may no longer respond until reloaded. Reload 🗙