Cellular damage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2001-11-16

AUTHORS

Gareth J Griffiths, Bernard M Corfe, Peter Savory, Sian Leech, Mauro Degli Esposti, John A Hickman, Caroline Dive

ABSTRACT

The pro-apoptotic protein Bak is converted from a latent to an active form by damage-induced signals. This process involves an early exposure of an occluded N-terminal epitope of Bak in intact cells. Here we report a subsequent damage-induced change in Bak, detected using an antibody to the central BH-1 domain. Bak co-immunoprecipitated with Bc1-xL both in undamaged cells and early after damage, when the N-terminal epitope was exposed but the BH-1 epitope remained occluded. A subsequent decrease in binding of Bak to Bc1-xL correlated with exposure of an epitope in the Bak BH-1 domain. Overexpression of Bc1-xL did not affect the kinetics of exposure of the Bak N-terminal epitope but delayed exposure of the BH-1 domain. Cytochrome c release from mitochondria facilitates the activation of apoptotic caspases. The majority of cells with exposed Bak BH-1 domains contained cytosolic cytochrome c. However, a small proportion of cells exhibited exposed Bak BH-1 domains that co-localized with mitochondrial cytochrome c. The data are consistent with a two-step model for the activation of Bak by drug-induced damage signals where dissociation of Bc1-xL from the BH-1 domain of Bak occurs immediately prior to or concomitantly with cytochrome c release. More... »

PAGES

7668-7676

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/sj.onc.1204995

DOI

http://dx.doi.org/10.1038/sj.onc.1204995

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1038746982

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11753644


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