期刊
JOURNAL OF CELL SCIENCE
卷 122, 期 10, 页码 1680-1690出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.036103
关键词
Brefeldin A; COPII; Endoplasmic reticulum; Membrane fusion; Subdomain; Syntaxin 18
类别
资金
- Ministry of Education, Science, Sports, and Culture of Japan [18570186, 1837008]
- Grants-in-Aid for Scientific Research [18570186] Funding Source: KAKEN
The presence of subdomains in the endoplasmic reticulum ( ER) enables this organelle to perform a variety of functions, yet the mechanisms underlying their organization are poorly understood. In the present study, we show that syntaxin 18, a SNAP (soluble NSF attachment protein) receptor localized in the ER, is important for the organization of two ER subdomains, smooth/rough ER membranes and ER exit sites. Knockdown of syntaxin 18 caused a global change in ER membrane architecture, leading to the segregation of the smooth and rough ER. Furthermore, the organization of ER exit sites was markedly changed concomitantly with dispersion of the ER-olgi intermediate compartment and the Golgi complex. These morphological changes in the ER were substantially recovered by treatment of syntaxin-18-depleted cells with brefeldin A, a reagent that stimulates retrograde membrane flow to the ER. These results suggest that syntaxin 18 has an important role in ER subdomain organization by mediating the fusion of retrograde membrane carriers with the ER membrane.
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