The Sec62/63 translocon facilitates membrane insertion and C-terminal translocation of multi-spanning membrane proteins

Majority of membrane proteins are co-translationally translocated. The Sec62/Sec63 complex which mediates post-translational translocation of a subset of primarily secretory proteins into the endoplasmic reticulum (ER), therefore has been thought uninvolved in targeting and translocation of membrane proteins. By systematic analysis of single and multi-spanning membrane proteins with broad sequence context; varying hydrophobicity, flanking charged residues and orientation of transmembrane (TM) segments, in a set of Sec62 mutant yeast strains, we show that mutations in the N-terminal cytosolic domain of Sec62 impair interaction with Sec63 and lead to defects in membrane insertion and the C-terminal translocation of membrane proteins. These results reveal an unappreciated function of the Sec62/Sec63 translocon as a general membrane chaperone that regulates topogenesis of membrane proteins in the eukaryotic cell.

Kim, HaniSeoul National University (författare)
Reithinger, Johannes HStockholms universitet,Institutionen för biokemi och biofysik(Swepub:su)jreit (författare)
Kim, HyunSeoul National University, Seoul, South Korea (författare)
Seoul National University, Seoul, South KoreaSeoul National University (creator_code:org_t)

Av författaren/redakt...: Jung, Sung-jun; Kim, Hani; Reithinger, Joha ...; Kim, Hyun

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