Post-Translational Protein Transport by the Sec Complex

William J Allen; Ian Collinson; Karin Römisch

doi:10.1016/j.tibs.2019.03.003

Post-Translational Protein Transport by the Sec Complex

Trends Biochem Sci. 2019 Jun;44(6):481-483. doi: 10.1016/j.tibs.2019.03.003. Epub 2019 Apr 5.

Authors

William J Allen¹, Ian Collinson¹, Karin Römisch²

Affiliations

¹ School of Biochemistry, University of Bristol, Bristol, UK.
² Faculty of Natural Sciences and Technology, Saarland University, Saarbruecken, Germany. Electronic address: k.roemisch@mx.uni-saarland.de.

PMID: 30962027
DOI: 10.1016/j.tibs.2019.03.003

Abstract

Although it has been studied for 30 years, the mechanism by which secretory proteins are transported post-translationally into the endoplasmic reticulum (ER) has not yet been fully resolved. Recently published structures (Itskanov and Park, Science 2019;363:84-87; Wu, X. et al. Nature 2019;566:136-139) of the heptameric secretory (Sec) complex which mediates post-translational import into the yeast ER shed new light on the process.

Publication types

Comment

MeSH terms

Membrane Transport Proteins*
Protein Transport
SEC Translocation Channels
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins*

Substances

Membrane Transport Proteins
SEC Translocation Channels
Saccharomyces cerevisiae Proteins