Affordable Access

deepdyve-link
Publisher Website

Ubiquitination of Rac1 by inhibitors of apoptosis (IAPs).

Authors
  • Oberoi-Khanuja, Tripat Kaur
  • Rajalingam, Krishnaraj
Type
Published Article
Journal
Methods in Molecular Biology
Publication Date
Jan 01, 2014
Volume
1120
Pages
43–54
Identifiers
DOI: 10.1007/978-1-62703-791-4_4
PMID: 24470018
Source
Medline
License
Unknown

Abstract

Ubiquitination of proteins has emerged as a vital posttranslational modification at the crux of numerous signalling pathways, regulating them in various ways. Most members of the small GTPase family including Ras and Rho proteins are regulated by GEFs, GAPs, and RhoGDIs that modulate their cycling between the active and inactive states. Ubiquitination has added another layer to the regulation of small GTPases. Recently, we have uncovered that inhibitors of apoptosis (IAPs) function as direct E3 ubiquitin ligases for Rho GTPase Rac1 and target it for proteasomal degradation. Here, we describe in vitro and in vivo ubiquitination assays for detecting the conjugation of ubiquitin to Rac1 by XIAP and cIAP1.

Report this publication

Statistics

Seen <100 times