An ER surface retrieval pathway safeguards the import of mitochondrial membrane proteins in yeast

Science
Katja G HansenJ M Herrmann

Abstract

The majority of organellar proteins are translated on cytosolic ribosomes and must be sorted correctly to function. Targeting routes have been identified for organelles such as peroxisomes and the endoplasmic reticulum (ER). However, little is known about the initial steps of targeting of mitochondrial proteins. In this study, we used a genome-wide screen in yeast and identified factors critical for the intracellular sorting of the mitochondrial inner membrane protein Oxa1. The screen uncovered an unexpected path, termed ER-SURF, for targeting of mitochondrial membrane proteins. This pathway retrieves mitochondrial proteins from the ER surface and reroutes them to mitochondria with the aid of the ER-localized chaperone Djp1. Hence, cells use the expanse of the ER surfaces as a fail-safe to maximize productive mitochondrial protein targeting.

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Citations

Oct 31, 2018·Nature Structural & Molecular Biology·Johannes M HerrmannTohru Yoshihisa
Jun 13, 2019·The Protein Journal·Yuanyuan ChenRoss E Dalbey
Oct 11, 2019·Nucleic Acids Research·Martine A Collart, Benjamin Weiss
Feb 6, 2020·Biological Chemistry·Layla Drwesh, Doron Rapaport
Mar 7, 2020·Biological Chemistry·Maria Clara Avendaño-MonsalveSoledad Funes
May 26, 2020·EMBO Reports·Raz Bar-ZivAndrew Dillin
Jan 23, 2020·Biological Chemistry·Alexander Grevel, Thomas Becker
Aug 28, 2020·The Biochemical Journal·Karthik MohanrajAgnieszka Chacinska
Apr 28, 2019·Journal of Cell Science·Ulrike TopfAgnieszka Chacinska
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