ER-associated Protein Degradation at Atomic Resolution

Mohamed A Eldeeb; Richard P Fahlman; Marek Michalak

doi:10.1016/j.tibs.2020.06.005

ER-associated Protein Degradation at Atomic Resolution

Trends Biochem Sci. 2020 Sep;45(9):723-725. doi: 10.1016/j.tibs.2020.06.005.

Authors

Mohamed A Eldeeb¹, Richard P Fahlman², Marek Michalak³

Affiliations

¹ McGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, QC, H3A 2B4, Canada. Electronic address: mohamed.eldeeb@mcgill.ca.
² Department of Biochemistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada. Electronic address: rfahlman@ualberta.ca.
³ Department of Biochemistry, University of Alberta, Edmonton, AB, T6G 2H7, Canada. Electronic address: marek.michalak@ualberta.ca.

PMID: 32616332
DOI: 10.1016/j.tibs.2020.06.005

Abstract

The endoplasmic reticulum-associated degradation (ERAD) pathway eliminates misfolded proteins. The Hrd1 complex represents the main gate mediating retrotranslocation of ER luminal misfolded (ERAD-L) substrates to the cytosol. A recent cryo-electron microscopy (cryo-EM) study by Wu et al. unveils the structural features of active Hrd1, providing mechanistic insights into the movement of proteins directed for degradation across ER membranes.

Keywords: ERAD; HRD1 complex; cryo-EM; endoplasmic reticulum; proteasome; protein degradation; protein quality control; ubiquitin.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Cryoelectron Microscopy*
Endoplasmic Reticulum / metabolism
Endoplasmic Reticulum-Associated Degradation*
Proteolysis
Ubiquitin-Protein Ligases / metabolism
Ubiquitins / metabolism

Substances

Ubiquitins
Ubiquitin-Protein Ligases