Reference: Jung SJ, et al. (2014) The Sec62-Sec63 translocon facilitates translocation of the C-terminus of membrane proteins. J Cell Sci 127(Pt 19):4270-8

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Abstract


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.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Jung SJ, Kim JE, Reithinger JH, Kim H
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