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• W4313251151 abstract "The Ufd1/Npl4/Cdc48 complex is a universal protein segregase that plays key roles in eukaryotic cellular processes. Its functions orchestrating the clearance or removal of polyubiquitylated targets are established; however, prior studies suggest that the complex also targets substrates modified by the ubiquitin-like protein SUMO. Here, we show that interactions between Ufd1 and SUMO enhance unfolding of substrates modified by SUMO-polyubiquitin hybrid chains by the budding yeast Ufd1/Npl4/Cdc48 complex compared to substrates modified by polyubiquitin chains, a difference that is accentuated when the complex has a choice between these substrates. Incubating Ufd1/Npl4/Cdc48 with a substrate modified by a SUMO-polyubiquitin hybrid chain produced a series of single-particle cryo-EM structures that reveal features of interactions between Ufd1/Npl4/Cdc48 and ubiquitin prior to and during unfolding of ubiquitin. These results are consistent with cellular functions for SUMO and ubiquitin modifications and support a physical model wherein Ufd1/Npl4/Cdc48, SUMO, and ubiquitin conjugation pathways converge to promote clearance of proteins modified with SUMO and polyubiquitin." @default.
• W4313251151 created "2023-01-06" @default.
• W4313251151 creator A5013774625 @default.
• W4313251151 creator A5020529342 @default.
• W4313251151 creator A5049229227 @default.
• W4313251151 date "2022-12-27" @default.
• W4313251151 modified "2023-09-26" @default.
• W4313251151 title "SUMO enhances unfolding of SUMO–polyubiquitin-modified substrates by the Ufd1/Npl4/Cdc48 complex" @default.
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• W4313251151 doi "https://doi.org/10.1073/pnas.2213703120" @default.
• W4313251151 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36574706" @default.
• W4313251151 hasPublicationYear "2022" @default.
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