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

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.
Mesh Terms:
Electron Transport Complex IV, Endoplasmic Reticulum, Membrane Proteins, Metabolic Networks and Pathways, Mitochondria, Mitochondrial Proteins, Molecular Chaperones, Nuclear Proteins, Protein Transport, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Science
Date: Dec. 14, 2017
Download Curated Data For This Publication
213914
Switch View:
  • Interactions 4