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Specific interaction of the antiapoptotic protein Nr-13 with phospholipid monolayers is prevented by the BH3 domain of Bax.

Abstract：

:Members of the Bcl-2 protein family regulate apoptosis by controlling the release of apoptogenic proteins such as cytochrome c from the mitochondrial intermembrane space. Proapoptotic members induce release by increasing outer membrane permeability, while antiapoptotic members prevent this. The activity of Bcl-2 proteins depends mostly on their insertion into the mitochondrial membrane, which is reported to occur via putative channels formed by the two central hydrophobic helices. The pro- and antiapoptotic activity of Bcl-2 proteins can also be modulated by heterodimerization between antagonists through the BH3 domain of proapoptotic members, though the position of the heterodimer with respect to the membrane has never been elucidated. In this work, the membrane insertion capacity of the antiapoptotic Bcl-2 related protein Nr-13 was explored, using monolayer expansion measurements. Nr-13 penetrates into the monolayer with a molecular cross-section of 1100A(2), thereby implicating almost all alpha-helical domains of the molecule in this process. A mutant protein, bearing neutral instead of acidic residues in the loop between the two putative channel-forming fifth and sixth alpha-helices, retained the ability to interact with the lipid monolayer, suggesting that the membrane insertion of Nr-13 is not exclusively alpha5-alpha6-dependent. In contrast, the specific interaction of Nr-13 with the monolayer was prevented by heterodimer formation with the BH3 domain of proapoptotic Bax. These findings are discussed in terms of a model for monolayer insertion in which the antiapoptotic Nr-13 and proapoptotic proteins exert their antagonistic effects by preventing each other from reaching the membrane.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Girard-Egrot A,Chauvet JP,Gillet G,Moradi-Améli M

doi

10.1016/j.jmb.2003.10.028

keywords:

subject

Has Abstract

pub_date

2004-01-02 00:00:00

pages

321-31

issue

1

eissn

0022-2836

issn

1089-8638

pii

S0022283603012968

journal_volume

335

pub_type

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