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Vol. 10, Issue 1, 119-134, January 1999
*Institute of Molecular and Cell Biology, Singapore 117609, Singapore; and
Syntaxin 1, synaptobrevins or vesicle-associated membrane proteins,
and the synaptosome-associated protein of 25 kDa (SNAP-25) are key
molecules involved in the docking and fusion of synaptic vesicles with
the presynaptic membrane. We report here the molecular, cell
biological, and biochemical characterization of a 32-kDa protein
homologous to both SNAP-25 (20% amino acid sequence identity) and the
recently identified SNAP-23 (19% amino acid sequence identity). Northern blot analysis shows that the mRNA for this protein is widely
expressed. Polyclonal antibodies against this protein detect a 32-kDa
protein present in both cytosol and membrane fractions. The
membrane-bound form of this protein is revealed to be primarily localized to the Golgi apparatus by indirect immunofluorescence microscopy, a finding that is further established by electron microscopy immunogold labeling showing that this protein is present in
tubular-vesicular structures of the Golgi apparatus. Biochemical characterizations establish that this protein behaves like a SNAP receptor and is thus named Golgi SNARE of 32 kDa (GS32). GS32 in the
Golgi extract is preferentially retained by the immobilized GST-syntaxin 6 fusion protein. The coimmunoprecipitation of syntaxin 6 but not syntaxin 5 or GS28 from the Golgi extract by antibodies against
GS32 further sustains the preferential interaction of GS32 with Golgi
syntaxin 6.
European Molecular Biology Laboratory, 69 Heidelberg, Germany
Corresponding author. E-mail
address: mcbhwj{at}imcb.nus.edu.sg.
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