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- W3206285936 endingPage "109840" @default.
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- W3206285936 abstract "Nearly one-third of proteins are initially targeted to the endoplasmic reticulum (ER) membrane, where they are correctly folded and then delivered to their final cellular destinations. To prevent the accumulation of misfolded membrane proteins, ER-associated degradation (ERAD) moves these clients from the ER membrane to the cytosol, a process known as retrotranslocation. Our recent work in Saccharomyces cerevisiae reveals a derlin rhomboid pseudoprotease, Dfm1, is involved in the retrotranslocation of ubiquitinated ERAD membrane substrates. In this study, we identify conserved residues of Dfm1 that are critical for retrotranslocation. We find several retrotranslocation-deficient Loop 1 mutants that display impaired binding to membrane substrates. Furthermore, Dfm1 possesses lipid thinning function to facilitate in the removal of ER membrane substrates, and this feature is conserved in its human homolog, Derlin-1, further implicating that derlin-mediated retrotranslocation is a well-conserved process." @default.
- W3206285936 created "2021-10-25" @default.
- W3206285936 creator A5000138383 @default.
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- W3206285936 creator A5081948146 @default.
- W3206285936 date "2021-10-01" @default.
- W3206285936 modified "2023-10-13" @default.
- W3206285936 title "Derlin rhomboid pseudoproteases employ substrate engagement and lipid distortion to enable the retrotranslocation of ERAD membrane substrates" @default.
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- W3206285936 doi "https://doi.org/10.1016/j.celrep.2021.109840" @default.
- W3206285936 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8641752" @default.
- W3206285936 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34686332" @default.
- W3206285936 hasPublicationYear "2021" @default.
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