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J Biol Chem, Vol. 273, Issue 12, 6944-6950, March 20, 1998
From the Membrane Biology Laboratory, Institute of Molecular and
Cell Biology, Singapore 117609, Republic of Singapore
We have cloned a new member of the syntaxin
family of proteins. The open reading frame encodes a polypeptide of 272 amino acids with potential coiled-coil domains and a C-terminal
hydrophobic tail. Northern blot analysis showed that the transcript is
fairly ubiquitous. A soluble recombinant form of the polypeptide
without the hydrophobic region binds to 
-SNAP (soluble
N-ethylmaleimide-sensitive factor attachment protein) and
syndet/SNAP-23 in vitro. Polyclonal antibody raised against
the recombinant protein recognized a 39-kDa protein in the membrane
fraction of cell lysates. Indirect immunofluorescence studies using the
polyclonal antibody showed that the protein is localized to
intracellular membrane structures. Selective permeabilization studies
with digitonin and saponin indicate that the epitope(s) recognized by
the antibody is expose to the cytoplasm, consistent with the predicted
orientation characteristic of SNAP receptor molecules. Morphological
alterations of the staining pattern of the protein with brefeldin A and
wortmannin treatment indicate that the protein is localize to the
endosome. The cDNA we have cloned apparently corresponded to three
previously described expressed sequence tags named as syntaxins 12, 13, and 14, respectively. We therefore propose to retain the name syntaxin
12 for this protein.
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