A role of complexin-lipid interactions in membrane fusion

被引:55
作者
Seiler, Florian [1 ]
Malsam, Joerg [1 ]
Krause, Jean Michel [1 ]
Soellner, Thomas H. [1 ]
机构
[1] Univ Heidelberg, Biochem Ctr, D-69120 Heidelberg, Germany
基金
美国国家卫生研究院;
关键词
Exocytosis; Fusion; SNARE; NEUROTRANSMITTER RELEASE; DISTINCT DOMAINS; SNARE COMPLEXES; EXOCYTOSIS; PROTEINS; SYNAPTOTAGMIN; BINDING;
D O I
10.1016/j.febslet.2009.06.025
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Complexins (Cpxs) and synaptotagmins regulate calcium-dependent exocytosis. A central helix in Cpx confers specific binding to the soluble N-ethylmaleimide-sensitive factor-attachment protein receptor (SNARE) fusion machinery. An accessory helix in the amino-terminal region inhibits membrane fusion by blocking SNAREpin zippering. We now show that an amphipathic helix in the carboxy-terminal region of CpxI binds lipid bilayers and affects SNARE-mediated lipid mixing in a liposome fusion assay. The substitution of a hydrophobic amino acid within the helix by a charged residue abolishes the lipid interaction and the stimulatory effect of CpxI in liposome fusion. In contrast, the introduction of the bulky hydrophobic amino acid tryptophan stimulates lipid binding and liposome fusion. This data shows that local Cpx-lipid interactions can play a role in membrane fusion. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
引用
收藏
页码:2343 / 2348
页数:6
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