Taking out the trash: How misfolded proteins are removed from the endoplasmic reticulum

Item Type:	Comment
Title:	Taking out the trash: How misfolded proteins are removed from the endoplasmic reticulum
Creators Name:	Brodsky, J.L. and Engelman, D.M. and Hendershot, L.M. and Piana-Agostinetti, S. and Sommer, T.
Abstract:	Proteins that are expressed on membrane surfaces or secreted are involved in all aspects of cellular and organismal life, and as such require extremely high fidelity during their synthesis and maturation. These proteins are synthesized at the endoplasmic reticulum (ER) where a dedicated quality control system (ERQC) ensures only properly matured proteins reach their destinations. An essential component of this process is the identification of proteins that fail to pass ERQC and their retrotranslocation to the cytosol for proteasomal degradation. This study by Wu et al. reports a cryo-electron microscopy (cryo-EM) structure of the five-protein channel through which aberrant proteins are extracted from the ER, providing insights into how recognition of misfolded proteins is coupled to their transport through a hydrophobic channel that acts to thin the ER membrane, further facilitating their dislocation to the cytosol.
Keywords:	Cryo-EM, ERAD, Endoplasmic Reticulum, Hrd1
Source:	Faculty Reviews
ISSN:	2732-432X
Publisher:	F1000 Research
Volume:	11
Page Range:	29
Date:	5 October 2022
Additional Information:	Copyright © 2022 Faculty Opinions Ltd.
Official Publication:	https://doi.org/10.12703/r-01-0000018
External Fulltext:	View full text on PubMed Central
PubMed:	View item in PubMed

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