A New Syntaxin Family Member Implicated in Targeting of Intracellular Transport Vesicles*
- From the Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University Medical Center, Stanford, California 94305-5428
- § Investigator of the Howard Hughes Medical Institute. To whom correspondence should be addressed. Tel.: 415-723-9075; Fax: 415-725-4436.
Abstract
Despite the central role vesicular trafficking occupies in protein targeting, the molecular coding of the trafficking signals and the mechanism of vesicle docking and fusion are just beginning to be understood. We report here the cloning and initial characterization of a new member of the syntaxin family of vesicular transport receptors. Syntaxin 6 is a 255-amino acid protein with two domains predicted to form coiled-coils, as well as a carboxyl-terminal membrane anchor. Syntaxin 6 is broadly expressed and localizes in the region of the Golgi apparatus. In vitro binding studies established that syntaxin 6 binds to α-soluble NSF attachment protein (α-SNAP). The sequence homology, topology, localization, and α-SNAP binding suggest that syntaxin 6 is involved in intracellular vesicle trafficking.
Footnotes
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↵‡ Medical Scientist Training Program student supported by National Institutes of Health General Medical Sciences Grant 5T32GM07365.
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↵* This work was supported in part by a grant from the National Institute of Mental Health. The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
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↵1 The abbreviations used are:
- SNARE
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soluble NSF attachment protein receptor
- NSF
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N-ethylmaleimide-sensitive factor
- SNAP
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soluble NSF attachment protein
- SNAP-25
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synapse-associated protein of 25 kDa
- EST
-
expressed sequence tag
- VAMP
-
vesicle-associated membrane protein
- kb
-
kilobase(s).
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- Received March 5, 1996.
- Revision received May 6, 1996.
- © 1996 by The American Society for Biochemistry and Molecular Biology, Inc.
