SYNTAXIN-10 - A MEMBER OF THE SYNTAXIN FAMILY LOCALIZED TO THE TRANS-GOLGI NETWORK

We have cloned a new member of the syntaxin family of proteins, design ated human syntaxin 10 (hsyn10). The open reading frame encodes a poly peptide of 249 amino acids with potential coiled-coil domains and a ca rboxy-terminal hydrophobic tail. hsyn10 is particularly homologous to the recently reported rat syntaxin 6 (about 60% identity). Northern bl ot analysis showed that the transcript is enriched in the heart, skele tal muscles and pancreas. indirect immunofluorescence studies using po lyclonal antibodies raised against recombinant protein showed that the protein is localized to intracellular membrane structures, with perin uclear staining patterns colocalising well with the Golgi SNARE GS28. Morphological alterations of the staining pattern of the protein with brefeldin A but not wortmannin treatment indicate that the protein is localize to the trans-Golgi network. (C) 1998 Academic Press.