Abstract
Bet1p is a type II membrane protein that is required for vesicular transport between the endoplasmic reticulum and Golgi complex in the yeast Saccharomyces cerevisiae. A domain of Bet1p, that shows potential to be involved in a coiled-coil interaction, is homologous to a region of the neuronal protein SNAP-25. Here, we used in vitro binding studies to demonstrate that Bet1p plays a role in potentiating soluble NSF attachment protein receptor (SNARE) interactions. Mutational analysis points to the coiled-coil region as necessary for Bet1p function, and circular dichroism experiments support this theory. In vitro binding studies were also used to demonstrate that a direct interaction between Bet1p and Bos1p is required for the efficient interaction of the vesicle SNARE with its SNARE target. Genetic studies suggest that the interactions of Bet1p with Bos1p are regulated by the small GTP-binding protein Ypt1p.
MeSH Terms
Amino Acid Sequence
Animals
Carrier Proteins/chemistry,genetics,metabolism
Cricetinae
Drug Synergism
Fungal Proteins/biosynthesis,chemistry,physiology
Humans
Membrane Proteins/biosynthesis,chemistry,genetics,metabolism,physiology
Membrane Transport Proteins
Molecular Sequence Data
Nerve Tissue Proteins/chemistry,genetics
Protein Structure, Secondary
Qb-SNARE Proteins
Qc-SNARE Proteins
SNARE Proteins
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Sequence Homology, Amino Acid
Synaptosomal-Associated Protein 25
Vesicular Transport Proteins
Chemicals
BET1 protein, S cerevisiae
BOS1 protein, S cerevisiae
Carrier Proteins
Fungal Proteins
Membrane Proteins
Membrane Transport Proteins
Nerve Tissue Proteins
Qb-SNARE Proteins
Qc-SNARE Proteins
SNAP25 protein, human
SNARE Proteins
Saccharomyces cerevisiae Proteins
Synaptosomal-Associated Protein 25
Vesicular Transport Proteins
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Stone S
Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
Sacher M
Mao Y
Carr C
Lyons P
Quinn A M
Ferro-Novick S
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