Ontology highlight
ABSTRACT:
SUBMITTER: Maiuri MC
PROVIDER: S-EPMC1868901 | biostudies-other | 2007 May
REPOSITORIES: biostudies-other
Maiuri M Chiara MC Le Toumelin Gaëtane G Criollo Alfredo A Rain Jean-Christophe JC Gautier Fabien F Juin Philippe P Tasdemir Ezgi E Pierron Gérard G Troulinaki Kostoula K Tavernarakis Nektarios N Hickman John A JA Geneste Olivier O Kroemer Guido G
The EMBO journal 20070419 10
The anti-apoptotic proteins Bcl-2 and Bcl-X(L) bind and inhibit Beclin-1, an essential mediator of autophagy. Here, we demonstrate that this interaction involves a BH3 domain within Beclin-1 (residues 114-123). The physical interaction between Beclin-1 and Bcl-X(L) is lost when the BH3 domain of Beclin-1 or the BH3 receptor domain of Bcl-X(L) is mutated. Mutation of the BH3 domain of Beclin-1 or of the BH3 receptor domain of Bcl-X(L) abolishes the Bcl-X(L)-mediated inhibition of autophagy trigge ...[more]