期刊
JOURNAL OF CELL SCIENCE
卷 127, 期 19, 页码 4270-4278出版社
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.153650
关键词
Endoplasmic reticulum; ER; Co-translational translocation; Sec61; Topology; Yeast
类别
资金
- National Research Foundation of Korea [2012-0001935, C00048]
The Sec62-Sec63 complex mediates post-translational translocation of a subset of primarily secretory proteins into the endoplasmic reticulum (ER) in yeast. Therefore, it has been thought that membrane proteins, which are mainly co-translationally targeted into the ER, are not handled by the Sec62-Sec63 translocon. By systematic analysis of single and multi-spanning membrane proteins with broad sequence context [with differing hydrophobicity, flanking charged residues and orientation of transmembrane (TM) segments], we show that mutations in the N-terminal cytosolic domain of yeast Sec62 impair its interaction with Sec63 and lead to defects in membrane insertion and translocation of the C-terminus of membrane proteins. These results suggest that there is an unappreciated function of the Sec62-Sec63 translocon in regulating topogenesis of membrane proteins in the eukaryotic cell.
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