期刊
JOURNAL OF CELL SCIENCE
卷 136, 期 9, 页码 -出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.261094
关键词
Endoplasmic reticulum; ER; COPII; ER exit sites; Sec16; Sed4
类别
COPII proteins assemble at ER exit sites to form transport carriers. Sec12 triggers the initiation of COPII assembly in yeast and Sec16 plays a critical role in COPII organization. We found that a Sec12 homolog, Sed4, concentrates at ERES and mediates the ERES localization of Sec16. Our findings provide insight into the interdependent function of Sec16 and Sed4 at ERES.
COPII proteins assemble at ER exit sites (ERES) to form transport carriers. The initiation of COPII assembly in the yeast Saccharomyces cerevisiae is triggered by the ER membrane protein Sec12. Sec16, which plays a critical role in COPII organization, localizes to ERES independently of Sec12. However, the mechanism underlying Sec16 localization is poorly understood. Here, we show that a Sec12 homolog, Sed4, is concentrated at ERES and mediates ERES localization of Sec16. We found that the interaction between Sec16 and Sed4 ensures their correct localization to ERES. Loss of the interaction with Sec16 leads to redistribution of Sed4 from the ERES specifically to high-curvature ER areas, such as the tubules and edges of the sheets. The luminal domain of Sed4 mediates this distribution, which is required for Sed4, but not for Sec16, to be concentrated at ERES. We further show that the luminal domain and its O-mannosylation are involved in the self -interaction of Sed4. Our findings provide insight into how Sec16 and Sed4 function interdependently at ERES.
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