Syntaxin-16, a putative Golgi t-SNARE.
Members of the syntaxin family of integral membrane proteins have recently been implicated as vesicle receptors on target membranes, coresponsible for the specificity of intracellular membrane traffic. So far, only a small number of different mammalian syntaxins have been identified. Here we report the cloning of three new human syntaxin cDNAs, presumably originating from alternative splicing of the same transcript. Syntaxin- 16A and syntaxin-16B are identical, except that the latter contains an insertion of 21 amino acid residues. Syntaxin-16C is a truncated version of syntaxin- 16A, lacking the C-terminal coiled-coil and hydrophobic regions characteristic for syntaxins. Database searches identified putative yeast, plant and nematode homologues of syntaxin-16, indicating that this protein is conserved through evolution, and syntaxin-16 belongs to a new subgroup of syntaxins. Epitope-tagged syntaxin- 16A and syntaxin-16B were found to colocalize with the Golgi marker beta-COP, while syntaxin-16C was found in the cytosol. Syntaxin- 16A associates posttranslationally with microsomes, and appears to be transported to the Golgi via the endoplasmic reticulum. The three syntaxin-16 forms may have differential roles in intracellular trafficking.[1]References
- Syntaxin-16, a putative Golgi t-SNARE. Simonsen, A., Bremnes, B., Rønning, E., Aasland, R., Stenmark, H. Eur. J. Cell Biol. (1998) [Pubmed]
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