A role of complexin-lipid interactions in membrane fusion
| Autor: | Jean Michel Krause, Jörg Malsam, Thomas H. Söllner, Florian Seiler |
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| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Lipid Bilayers
Molecular Sequence Data Biophysics Nerve Tissue Proteins Biology Biochemistry Membrane Fusion Exocytosis Article Synaptotagmins 03 medical and health sciences Complexin Structural Biology Genetics Syntaxin Animals Humans Amino Acid Sequence Lipid bilayer Fusion Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences Liposome Sequence Homology Amino Acid 030302 biochemistry & molecular biology Lipid bilayer fusion Cell Biology Lipids Amino acid Adaptor Proteins Vesicular Transport chemistry SNARE Liposomes SNARE Proteins Sequence Alignment |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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