Molecular cloning and localization of human syntaxin 16, a member of the syntaxin family of SNARE proteins.

Abstract

We have cloned a new member of the syntaxin family of proteins, designated human syntaxin 16 (hsyn16). The open reading frame encodes a polypeptide of 307 amino acids with potential coiled-coil domains and a carboxy-terminal hydrophobic tail, which is characteristic of other members of the syntaxin family. The encoded polypeptide bears sequence homology to known syntaxin molecules. Northern blot analysis revealed a single transcript that is fairly ubiquitous, being slightly more enriched in heart and pancreas. Indirect immunofluorescence localised myc-tagged hsyn16 (myc-hsyn16) to the Golgi apparatus, colocalizing well with lens culinaris agglutinin, an established Golgi marker, as well as with other Golgi SNAREs such as GS28 and syntaxin 5. Myc-hsyn16 is redistributed to the endoplasmic reticulum upon brefeldin A treatment, indicating that it is localised to the Golgi stack. The ubiquitous expression and Golgi localization of hsy16 suggest that it is involved in a vesicular transport step within the organelle.

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@article{Tang1998MolecularCA, title={Molecular cloning and localization of human syntaxin 16, a member of the syntaxin family of SNARE proteins.}, author={Bor Luen Tang and Dorrain Y Low and S. S. Lee and Ay Eeng Tan and Wan Jing Hong}, journal={Biochemical and biophysical research communications}, year={1998}, volume={242 3}, pages={673-9} }