Journal Article

DKFZ-2017-00042

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Pro-apoptotic cBid and Bax exhibit distinct membrane remodeling activities: An AFM study.

Unsay, J. D. (First author)DKFZ* ; Cosentino, K. ; Sporbeck, K. ; García-Sáez, A. J.

2017
Elsevier Amsterdam

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Please use a persistent id in citations: doi:10.1016/j.bbamem.2016.10.007

Abstract: Bcl-2 proteins are key regulators of the mitochondrial outer membrane (MOM) permeabilization that mediates apoptosis. During apoptosis, Bid is cleaved (cBid) and translocates to the MOM, where it activates Bax. Bax then oligomerizes and induces MOM permeabilization. However, little is known about how these proteins affect membrane organization aside from pore formation. In previous studies, we have shown that both cBid and Bax are able to remodel membranes and stabilize curvature. Here, we dissected the independent effects of Bax and cBid on supported lipid structures mimicking the mitochondrial composition by means of atomic force spectroscopy. We show that cBid did not permeabilize the membrane but lowered the membrane breakthrough force. On the other hand, Bax effects were dependent on its oligomeric state. Monomeric Bax did not affect the membrane properties. In contrast, oligomeric Bax lowered the breakthrough force of the membrane, which in the context of pore formation, implies a lowering of the line tension at the edge of the pore.

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Contributing Institute(s):

1. Membranbiophysik (B160)

Research Program(s):

1. 312 - Functional and structural genomics (POF3-312) (POF3-312)

Appears in the scientific report 2017

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Database coverage:
BIOSIS Previews ; Current Contents - Life Sciences ; Ebsco Academic Search ; IF < 5 ; JCR ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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