Journal article
Direct interaction between SNAP‐23 and L‐type Ca2+ channel
Abstract
During secretion, membrane-bound secretory vesicles dock and fuse at the base of porosomes in the cell plasma membrane. Among other proteins, the porosome is composed of SNAREs and Ca2+-channels. Ca2+-channels and SNAREs have been implicated in cell secretion. Several immunoprecipitation and binding studies suggest the physical interaction of the t-SNARE proteins, Syntaxin-1 and SNAP-25 with various Ca2+-channels. In this study, using yeast …
Authors
Cho WJ; Jeremic A; Jena BP
Journal
Journal of Cellular and Molecular Medicine, Vol. 9, No. 2, pp. 380–386
Publisher
Wiley
Publication Date
April 2005
DOI
10.1111/j.1582-4934.2005.tb00363.x
ISSN
1582-1838
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceAnimalsBase SequenceCalcium Channels, L-TypeCarrier ProteinsCell MembraneImmunoprecipitationMaleModels, MolecularPancreasProtein BindingQb-SNARE ProteinsQc-SNARE ProteinsRatsRats, Sprague-DawleySequence Homology, Amino AcidSequence Homology, Nucleic AcidTwo-Hybrid System TechniquesYeasts