Derlin rhomboid pseudoproteases employ substrate engagement and lipid distortion to enable the retrotranslocation of ERAD membrane substrates
Year: 2022
Type: article
Abstract: (Cell Reports 37, 109840, October 19, 2021) In the originally published version of this article, there was in error in Figures 5E and S1A. For Figure 5E, in the bottom panel for HA blot/input control, the blot was inadvertently cropped so that the panel had 15 lanes rather than the intended 16 lanes. For Figure S1A, there was an error in which Q101R and F107S HA blot was inadvertently used from the same HA blot for L64V and K67E. The original and corrected figures appear here, and the corrected figures now appear with the article online. The authors regret this error.Figure 5. Dfm1 L1 residues are required for binding to integral membrane substrates (original)View Large Image Figure ViewerDownload Hi-res image Download (PPT)Figure S1. Dfm1 is a rhomboid pseudoprotease (corrected)View Large Image Figure ViewerDownload Hi-res image Download (PPT)Figure S1. Dfm1 is a rhomboid pseudoprotease (original)View Large Image Figure ViewerDownload Hi-res image Download (PPT) Derlin rhomboid pseudoproteases employ substrate engagement and lipid distortion to enable the retrotranslocation of ERAD membrane substratesNejatfard et al.Cell ReportsOctober 19, 2021In BriefER-associated degradation is a conserved pathway of protein quality control that requires the retrotranslocation of ubiquitinated substrates from the ER to the cytoplasm for degradation. Nejatfard et al. show that derlin rhomboid pseudoproteases mediate the retrotranslocation of misfolded membrane substrates via a mechanism that is conserved from yeast to humans. Full-Text PDF Open Access
Source: Cell Reports
Language: English
Subfield: Cell Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $5,200
OpenAlex ID: W4220699171