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Size of supramolecular SNARE complex: membrane-directed self-assembly.

ABSTRACT: Full length v-SNARE protein in lipid vesicles when exposed to t-SNARE-reconstituted lipid membrane results in the self-assembly of a t-/v-SNARE complex in a ring pattern, forming pores, and establishing continuity between the opposing bilayers. It is known that smaller vesicles fuse more efficiently than larger ones, and hence the curvature of secretory vesicles may dictate the potency and efficacy of their fusion at the cell plasma membrane. The diameter of t- and v-SNARE vesicles may, therefore, reflect the size of the t-/v-SNARE complex formed. In the present study, this hypothesis was tested, and results from the study demonstrate that the size of the t-/v-SNARE complex is directly proportional to the vesicle diameter (R2 = 0.9725).

SUBMITTER: Cho WJ

PROVIDER: S-EPMC4580238 | biostudies-literature | 2005 Jul

REPOSITORIES: biostudies-literature

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Size of supramolecular SNARE complex: membrane-directed self-assembly.

Cho Won Jin WJ Jeremic Aleksandar A Jena Bhanu P BP

Journal of the American Chemical Society 20050701 29

Full length v-SNARE protein in lipid vesicles when exposed to t-SNARE-reconstituted lipid membrane results in the self-assembly of a t-/v-SNARE complex in a ring pattern, forming pores, and establishing continuity between the opposing bilayers. It is known that smaller vesicles fuse more efficiently than larger ones, and hence the curvature of secretory vesicles may dictate the potency and efficacy of their fusion at the cell plasma membrane. The diameter of t- and v-SNARE vesicles may, therefor ...[more]

PMID: 16028912

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