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Biochem J. 2003 Aug 1;373(Pt 3):965-71.

Identification of ubiquitination sites on the X-linked inhibitor of apoptosis protein.

Author information

1
The Program in Apoptosis and Cell Death Research, Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.

Abstract

The execution phase of apoptosis is under the control of members of the inhibitor of apoptosis (IAP) family of zinc finger proteins. Several of these proteins contain a C-terminal RING (really interesting new gene) domain that has been postulated to regulate ubiquitination of themselves or their target proteins, thereby modulating thresholds for apoptosis. We demonstrate that the auto-ubiquitination sites of the X-linked IAP (XIAP) are Lys(322) and Lys(328), located in the third baculovirus IAP repeat domain of the protein. Modification of these sites to arginine dramatically reduces ubiquitination of XIAP, but has no measurable effect on the ability of ectopically expressed IAP to rescue cells from two independent apoptotic inducers. Our data firmly locate the auto-ubiquitination sites, and raise doubts regarding the importance of this event as a mechanism for regulating the levels of XIAP.

PMID:
12747801
PMCID:
PMC1223557
DOI:
10.1042/BJ20030583
[Indexed for MEDLINE]
Free PMC Article

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