MOLECULAR-CLONING AND LOCALIZATION OF HUMAN SYNTAXIN-16, A MEMBER OF THE SYNTAXIN FAMILY OF SNARE PROTEINS

We have cloned a new member of the syntaxin family of proteins, design ated human syntaxin 16 (hsyn16), The open reading frame encodes a poly peptide of 307 amino acids with potential coiled-coil domains and a ca rboxy-terminal hydrophobic tail, which is characteristic of other memb ers of the syntaxin family. The encoded polypeptide bears sequence hom ology to known syntaxin molecules. Northern blot analysis revealed a s ingle transcript that is fairly ubiquitous, being slightly more more e nriched in heart and pancreas, Indirect immunofluorescence localised m yc-tagged hsyn16 (myc-hsyn16) to the Golgi apparatus, colocalizing wel l with lens culinaris agglutinin, an established Gels marker, as well as with other Gels SNAREs such as GS28 and syntaxin 5. Myc-hsyn16 is r edistributed to the endoplasmic reticulum upon brefeldin A treatment, indicating that it is localised to the Gels stack. The ubiquitous expr ession and Golgi localization of hsy16 suggest that it is involved in a vesicular transport step within the organelle. (C) 1998 Academic Pre ss.