{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kandel R"],"funding":["Pew Charitable Trusts","NHLBI NIH HHS","National Institute of General Medical Sciences","NIGMS NIH HHS","National Science Foundation"],"pagination":["e3001950"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9894555"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["21(1)"],"pubmed_abstract":["Protein aggregates are a common feature of diseased and aged cells. Membrane proteins comprise a quarter of the proteome, and yet, it is not well understood how aggregation of membrane proteins is regulated and what effects these aggregates can have on cellular health. We have determined in yeast that the derlin Dfm1 has a chaperone-like activity that influences misfolded membrane protein aggregation. We establish that this function of Dfm1 does not require recruitment of the ATPase Cdc48 and it is distinct from Dfm1's previously identified function in dislocating misfolded membrane proteins from the endoplasmic reticulum (ER) to the cytosol for degradation. Additionally, we assess the cellular impacts of misfolded membrane proteins in the absence of Dfm1 and determine that misfolded membr"],"journal":["PLoS biology"],"pubmed_title":["Yeast derlin Dfm1 employs a chaperone-like function to resolve misfolded membrane protein stress."],"pmcid":["PMC9894555"],"funding_grant_id":["R35 GM133565","T32 GM133351","34089","R00 GM135515","1R35GM133565","T32 HL007444","2047391","R00GM135515","R25 HL145817"],"pubmed_authors":["Songster L","Duttke S","Jung J","Chapman C","Benner C","Syau D","Horn C","Neal SE","Aguayo A","Kuo T","Kandel R"],"additional_accession":[]},"is_claimable":false,"name":"Yeast derlin Dfm1 employs a chaperone-like function to resolve misfolded membrane protein stress.","description":"Protein aggregates are a common feature of diseased and aged cells. Membrane proteins comprise a quarter of the proteome, and yet, it is not well understood how aggregation of membrane proteins is regulated and what effects these aggregates can have on cellular health. We have determined in yeast that the derlin Dfm1 has a chaperone-like activity that influences misfolded membrane protein aggregation. We establish that this function of Dfm1 does not require recruitment of the ATPase Cdc48 and it is distinct from Dfm1's previously identified function in dislocating misfolded membrane proteins from the endoplasmic reticulum (ER) to the cytosol for degradation. Additionally, we assess the cellular impacts of misfolded membrane proteins in the absence of Dfm1 and determine that misfolded membr","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-07-16T20:12:02.941Z","creation":"2025-04-06T02:21:17.733Z"},"accession":"S-EPMC9894555","cross_references":{"pubmed":["36689475"],"doi":["10.1371/journal.pbio.3001950"]}}