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The Sec62-Sec63 translocon facilitates translocation of the C-terminus of membrane proteins
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2014 (English)In: Journal of Cell Science, ISSN 0021-9533, E-ISSN 1477-9137, Vol. 127, no 19, 4270-4278 p.Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2014. Vol. 127, no 19, 4270-4278 p.
Keyword [en]
Endoplasmic reticulum, ER, Co-translational translocation, Sec61, Topology, Yeast
National Category
Cell Biology
URN: urn:nbn:se:su:diva-109278DOI: 10.1242/jcs.153650ISI: 000343123500016OAI: diva2:764839


Available from: 2014-11-20 Created: 2014-11-17 Last updated: 2014-11-20Bibliographically approved

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