{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Hunt LC"],"funding":["NIA NIH HHS"],"pubmed_abstract":["Ubiquitin-conjugating enzymes (E2s) are key for regulating protein function and turnover via ubiquitination but it remains undetermined which E2s maintain proteostasis during aging. Here, we find that E2s have diverse roles in handling a model aggregation-prone protein (huntingtin-polyQ) in the <i>Drosophila</i> retina: while some E2s mediate aggregate assembly, UBE2D/effete (eff) and other E2s are required for huntingtin-polyQ degradation. UBE2D/eff is key for proteostasis also in skeletal muscle: eff protein levels decline with aging, and muscle-specific eff knockdown causes an accelerated buildup in insoluble poly-ubiquitinated proteins (which progressively accumulate with aging) and shortens lifespan. Transgenic expression of human UBE2D2, homologous to eff, partially rescues the lifes"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2023.12.12.571303"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10759998"],"repository":["biostudies-literature"],"pubmed_title":["The ubiquitin-conjugating enzyme UBE2D/eff maintains a youthful proteome and ensures protein quality control during aging."],"pmcid":["PMC10759998"],"funding_grant_id":["R21 AG079267","RF1 AG068581","R01 AG055532"],"pubmed_authors":["Pagala V","Nyamkondiwa K","Kavdia K","Demontis F","Stephan A","Jiao J","Peng J","Hunt LC"],"additional_accession":[]},"is_claimable":false,"name":"The ubiquitin-conjugating enzyme UBE2D/eff maintains a youthful proteome and ensures protein quality control during aging.","description":"Ubiquitin-conjugating enzymes (E2s) are key for regulating protein function and turnover via ubiquitination but it remains undetermined which E2s maintain proteostasis during aging. Here, we find that E2s have diverse roles in handling a model aggregation-prone protein (huntingtin-polyQ) in the <i>Drosophila</i> retina: while some E2s mediate aggregate assembly, UBE2D/effete (eff) and other E2s are required for huntingtin-polyQ degradation. UBE2D/eff is key for proteostasis also in skeletal muscle: eff protein levels decline with aging, and muscle-specific eff knockdown causes an accelerated buildup in insoluble poly-ubiquitinated proteins (which progressively accumulate with aging) and shortens lifespan. Transgenic expression of human UBE2D2, homologous to eff, partially rescues the lifes","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Feb","modification":"2025-08-12T03:04:35.432Z","creation":"2025-08-12T03:04:35.432Z"},"accession":"S-EPMC10759998","cross_references":{"pubmed":["38168249"],"doi":["10.1101/2023.12.12.571303"]}}