The Sec62-Sec63 translocon facilitates translocation of the C-terminus of membrane proteins

AuthorCount:4;
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.

Kim, Ji Eun Hani (author)
Reithinger, Johannes H.Stockholms universitet,Institutionen för biokemi och biofysik (author)
Kim, Hyun (author)
Stockholms universitetInstitutionen för biokemi och biofysik (creator_code:org_t)

In:Journal of Cell Science: The Company of Biologists127:19, s. 4270-42780021-95331477-9137

By the author/editor: Jung, Sung-Jun; Kim, Ji Eun Hani; Reithinger, Joha ...; Kim, Hyun

About the subject

NATURAL SCIENCES: NATURAL SCIENCES; and Biological Scien ...; and Cell Biology

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