Three novel proteins of the syntaxin/SNAP-25 family.

Intracellular membrane traffic is thought to be regulated in part by soluble N-ethylmaleimide-sensitive factor-attachment protein receptors (SNAREs) through the formation of complexes between these proteins present on vesicle and target membranes. All known SNARE-mediated fusion events involve members of the syntaxin and vesicle-associated membrane protein families. The diversity of mammalian ...
membrane compartments predicts the existence of a large number of different syntaxin and vesicle-associated membrane protein genes. To further investigate the spectrum of SNAREs and their roles in membrane trafficking we characterized three novel members of the syntaxin and SNAP-25 (synaptosome-associated protein of 25 kDa) subfamilies. The proteins are broadly expressed, suggesting a general role in vesicle trafficking, and localize to distinct membrane compartments. Syntaxin 8 co-localizes with markers of the endoplasmic reticulum. Syntaxin 17, a divergent member of the syntaxin family, partially overlaps with endoplasmic reticulum markers, and SNAP-29 is broadly localized on multiple membranes. SNAP-29 does not contain a predicted membrane anchor characteristic of other SNAREs. In vitro studies established that SNAP-29 is capable of binding to a broad range of syntaxins.
Mesh Terms:
Amino Acid Sequence, Animals, Blotting, Northern, COS Cells, Cell Line, Databases, Factual, Endoplasmic Reticulum, Ethylmaleimide, Evolution, Molecular, Humans, Membrane Proteins, Molecular Sequence Data, Multigene Family, Nerve Tissue Proteins, Phylogeny, Qa-SNARE Proteins, Rats, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Synaptosomal-Associated Protein 25, Transfection
J. Biol. Chem.
Date: Dec. 18, 1998
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