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

BL Tang, DYH Low, S San Lee, AEH Tan… - … and biophysical research …, 1998 - Elsevier
BL Tang, DYH Low, S San Lee, AEH Tan, W Hong
Biochemical and biophysical research communications, 1998Elsevier
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 more enriched in heart and pancreas …
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 more enriched in heart and pancreas. Indirect immunofluorescence localised myc-tagged hsyn16 (myc-hsyn16) to the Golgi apparatus, colocalizing well withlens 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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