Hatsuzawa K, et al. (2000) (original) (raw)
Reference: Hatsuzawa K, et al. (2000)
Abstract
Members of the syntaxin family are target-soluble N-ethylmaleimide-sensitive factor-attachment protein receptors involved in vesicle docking and/or fusion within the exocytic and endocytotic pathways. By using the yeast two-hybrid system, we have identified a novel member of the syntaxin family, syntaxin 18, that binds to alpha-soluble N-ethylmaleimide-sensitive factor-attachment protein. Subcellular fractionation and immunocytochemical analysis revealed that syntaxin 18 is principally located in the endoplasmic reticulum. We examined the effect of overexpression of FLAG-tagged syntaxin 18 and a mutant lacking the N-terminal 81 amino acid residues on protein transport and organelles in the early secretory pathway. Both expressed proteins localized to the endoplasmic reticulum, and the expressed FLAG-syntaxin 18 caused remarkable aggregation of endoplasmic reticulum membranes. Although expression of the FLAG-syntaxin 18 lacking the N-terminal region produced less effect on the morphology of the endoplasmic reticulum, dispersion of the endoplasmic reticulum-Golgi intermediate compartment and cis-Golgi was elicited. Moreover, overexpression of the FLAG-syntaxin 18 mutant inhibited protein export from the endoplasmic reticulum. These results taken together suggest that syntaxin 18 functions in transport between the endoplasmic reticulum and Golgi.
PMID: 10788491
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Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Hatsuzawa K, Hirose H, Tani K, Yamamoto A, Scheller RH, Tagaya M
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