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

ER-associated Protein Degradation at Atomic Resolution

Mohamed A Eldeeb  1 , Richard P Fahlman  2 , Marek Michalak  3
Affiliations
Comment

ER-associated Protein Degradation at Atomic Resolution

Mohamed A Eldeeb et al. Trends Biochem Sci. 2020 Sep.

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.

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