title: 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).
authors: Department of Physiology, Wayne State University School of Medicine, Detroit, Michigan 48201, USA.
authors: Won Jin
authors: WJ
authors: Cho
authors: Aleksandar
authors: A
authors: Jeremic
authors: Bhanu P
authors: BP
authors: Jena
mesh_terms: D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism; D008567:Membranes, Artificial; D018625:Microscopy, Atomic Force; D050600:SNARE Proteins; D033921:Vesicular Transport Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D008051:Lipid Bilayers; D008567:Membranes, Artificial; D050600:SNARE Proteins; D033921:Vesicular Transport Proteins