Interaction of syntaxin with alpha-fodrin, a major component of the submembranous cytoskeleton - PubMed (original) (raw)
. 2001 Oct 26;288(2):468-75.
doi: 10.1006/bbrc.2001.5795.
Affiliations
- PMID: 11606066
- DOI: 10.1006/bbrc.2001.5795
Interaction of syntaxin with alpha-fodrin, a major component of the submembranous cytoskeleton
M Nakano et al. Biochem Biophys Res Commun. 2001.
Abstract
The soluble N-ethyl maleimide-sensitive factor attachment protein receptor machinery is involved in membrane docking and fusion. In this machinery, the syntaxin family is a central coordinator and participates in multiple protein-protein interactions. In this study we have shown that alpha-fodrin, nonerythroid spectrin, is a new binding partner of the syntaxin family. alpha-Fodrin bound to syntaxin-1a, -3, and -4, all of which are localized on the plasma membrane. Syntaxin-3 interacted with alpha-fodrin in dose-dependent and saturable manners but not with alpha-spectrin, erythroid spectrin. Syntaxin-3 interacted with alpha-fodrin through its C-terminal coiled-coil region. Binding of Munc18 or SNAP-25 to syntaxin-1a inhibited the interaction of alpha-fodrin with syntaxin-1a. Available evidence indicates that alpha-fodrin is implicated in exocytosis, but a precise mode of action of alpha-fodrin in exocytosis remains unclear. Our results suggest that alpha-fodrin regulates exocytosis through the interaction with members of the syntaxin family.
Copyright 2001 Academic Press.
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