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J Biol Chem, Vol. 275, Issue 18, 13713-13720, May 5, 2000
From the 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 The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AB028741.
Syntaxin 18, a SNAP Receptor That Functions in the
Endoplasmic Reticulum, Intermediate Compartment, and
cis-Golgi Vesicle Trafficking*
§,§,,
, and**
School of Life Science, Tokyo University of
Pharmacy and Life Science, Hachioji, Tokyo 192-0392, the
¶ Department of Physiology, Kansai Medical University,
Moriguchi, Osaka 570-8506, Japan, and Howard
Hughes Medical Institute, Department of Molecular and Cellular
Physiology, Stanford University Medical Center,
Stanford, California 94305-5428
-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.
*
This work was supported in part by Grants-in-aid from the
Ministry of Education, Science, Sports and Culture of Japan 09480165, 10215205, and 11480183, the Kato Memorial Bioscience Foundation, the
Naito Foundation, and the Uehara Memorial Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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