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Transmembrane-domain determinants for SNARE-mediated membrane fusion.

Fdez, Elena; Martínez-Salvador, Mar; Beard, Matthew; Woodman, Philip; Hilfiker, Sabine

Journal of cell science. 2010;123(Pt 14):2473-80.

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Abstract

Neurosecretion involves fusion of vesicles with the plasma membrane. Such membrane fusion is mediated by the SNARE complex, which is composed of the vesicle-associated protein synaptobrevin (VAMP2), and the plasma membrane proteins syntaxin-1A and SNAP-25. Although clearly important at the point of membrane fusion, the precise structural and functional requirements for the transmembrane domains (TMDs) of SNAREs in bringing about neurosecretion remain largely unknown. Here, we used a bimolecular fluorescence complementation (BiFC) approach to study SNARE protein interactions involving TMDs in vivo. VAMP2 molecules were found to dimerise through their TMDs in intact cells. Dimerisation was abolished when replacing a glycine residue in the centre of the TMD with residues of increasing molecular volume. However, such mutations still were fully competent in bringing about membrane-fusion events, suggesting that dimerisation of the VAMP2 TMDs does not have an important functional role. By contrast, a series of deletion or insertion mutants in the C-terminal half of the TMD were largely deficient in supporting neurosecretion, whereas mutations in the N-terminal half did not display severe secretory deficits. Thus, structural length requirements, largely confined to the C-terminal half of the VAMP2 TMD, seem to be essential for SNARE-mediated membrane-fusion events in cells.

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Place of publication:
England
Volume:
123
Issue:
Pt 14
Pagination:
2473-80
Digital Object Identifier:
10.1242/jcs.061325
Pubmed Identifier:
20571052
Pii Identifier:
jcs.061325
Access state:
Active

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Record metadata

Manchester eScholar ID:
uk-ac-man-scw:136822
Created by:
Woodman, Philip
Created:
17th November, 2011, 13:17:47
Last modified by:
Woodman, Philip
Last modified:
10th March, 2014, 14:52:45

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