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The Sec62/63 transl...
The Sec62/63 translocon facilitates membrane insertion and C-terminal translocation of multi-spanning membrane proteins
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- Jung, Sung-jun (author)
- Seoul National University, Seoul, South Korea
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- Kim, Hani (author)
- Seoul National University
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- Reithinger, Johannes H (author)
- Stockholms universitet,Institutionen för biokemi och biofysik
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- Kim, Hyun (author)
- Seoul National University, Seoul, South Korea
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(creator_code:org_t)
- English.
- Related links:
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https://urn.kb.se/re...
Abstract
Subject headings
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- 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.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- endoplasmic reticulum
- co-translational translocation
- Sec61
- topology
- yeast
Publication and Content Type
- vet (subject category)
- ovr (subject category)
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