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Title: Molecular cloning, expression analysis, and chromosomal localization of human syntaxin 8 (STX8). Author: Thoreau V, Bergès T, Callebaut I, Guillier-Gencik Z, Gressin L, Bernheim A, Karst F, Mornon JP, Kitzis A, Chomel JC. Journal: Biochem Biophys Res Commun; 1999 Apr 13; 257(2):577-83. PubMed ID: 10198254. Abstract: We report the cloning of a cDNA encoding human syntaxin 8 (STX8), using the regulator (R) domain of the cystic fibrosis transmembrane conductance regulator (CFTR) as a bait to screen a human fetal lung cDNA library by the yeast two-hybrid system. This gene was found broadly transcribed and its mRNA size is about 1.3 kb. The STX8 gene maps to chromosomal band 17p12 and it encodes a 236-amino-acid protein. Syntaxin 8 contains in its C-terminal half a coiled-coil domain found highly conserved in the t-SNARE (SNAP receptor on target membrane) superfamily of proteins, which are involved in vesicular trafficking and docking. In syntaxin 8, a C-terminal hydrophobic domain may constitute a transmembrane anchor. It was recently shown that CFTR-mediated chloride currents can be regulated by syntaxin 1A, a t-SNARE family member, through direct protein-protein interaction. This raises the possibility that syntaxin 8 may also be involved in such regulations.[Abstract] [Full Text] [Related] [New Search]