Work

Size of Supramolecular SNARE Complex: Membrane-Directed Self-Assembly

Year: 2005

Type: article

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).

Source: Journal of the American Chemical Society

DOI: 10.1021/ja052442m

Authors: Won Jin Cho, Aleksandar Jeremic, Bhanu P. Jena

Institution: Wayne State University

Language: English

Topic: Cellular transport and secretion

Subfield: Cell Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of Neurological Disorders and Stroke

Award: UNDERSTANDING MEMBRANE FUSION A BIOENGINEERING APPROACH