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J Biol Chem, Vol. 273, Issue 34, 21783-21789, August 21, 1998
From the Membrane Biology Laboratory, Institute of Molecular and
Cell Biology, Singapore 117609, Singapore
Expressed sequence tags coding for a potential
SNARE (soluble N-ethylmaleimide-sensitive factor attachment
protein receptor) were revealed during data base searches. The deduced
amino acid sequence of the complete coding region predicts a
217-residue protein with a COOH-terminal hydrophobic membrane anchor.
Affinity-purified antibodies raised against the cytoplasmic region of
this protein specifically detect a 29-kilodalton integral membrane
protein enriched in the Golgi membrane. Indirect immunofluorescence
microscopy reveals that this protein is mainly associated with the
Golgi apparatus. When detergent extracts of the Golgi membrane are
incubated with immobilized glutathione S-transferase 
soluble N-ethylmaleimide-sensitive factor attachment
protein (GST--SNAP), this protein was specifically retained. This
protein has been independently identified and termed Vti1-rp2, and it
is homologous to Vti1p, a yeast Golgi SNARE. We further show that
Vti1-rp2 can be qualitatively coimmunoprecipitated with Golgi syntaxin
5 and syntaxin 6, suggesting that Vti1-rp2 exists in at least two
distinct Golgi SNARE complexes. In cells microinjected with antibodies
against Vti1-rp2, transport of the envelope protein (G-protein) of
vesicular stomatitis virus from the endoplasmic reticulum to the plasma
membrane was specifically arrested at the Golgi apparatus, providing
further evidence for functional importance of Vti1-rp2 in protein
trafficking in the secretory pathway.
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