Identification of ubiquitination sites on the X-linked inhibitor of apoptosis protein.
Biochem J
; 373(Pt 3): 965-71, 2003 Aug 01.
Article
em En
| MEDLINE
| ID: mdl-12747801
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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas
/
Ubiquitina
Tipo de estudo:
Diagnostic_studies
/
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
Biochem J
Ano de publicação:
2003
Tipo de documento:
Article
País de afiliação:
Estados Unidos