{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["9(1)"],"submitter":["Tsuchiya H"],"pubmed_abstract":["Protein ubiquitylation regulates diverse cellular processes via distinct ubiquitin chains that differ by linkage type and length. However, a comprehensive method for measuring these properties has not been developed. Here we describe a method for assessing the length of substrate-attached polyubiquitin chains, \"ubiquitin chain protection from trypsinization (Ub-ProT).\" Using Ub-ProT, we found that most ubiquitylated substrates in yeast-soluble lysate are attached to chains of up to seven ubiquitin molecules. Inactivation of the ubiquitin-selective chaperone Cdc48 caused a dramatic increase in chain lengths on substrate proteins, suggesting that Cdc48 complex terminates chain elongation by substrate extraction. In mammalian cells, we found that ligand-activated epidermal growth factor recep"],"journal":["Nature communications"],"pagination":["524"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5802829"],"repository":["biostudies-literature"],"pubmed_title":["Ub-ProT reveals global length and composition of protein ubiquitylation in cells."],"pmcid":["PMC5802829"],"pubmed_authors":["Burana D","Saeki Y","Komada M","Ohtake F","Arai N","Kaiho A","Tanaka K","Tsuchiya H"],"additional_accession":[]},"is_claimable":false,"name":"Ub-ProT reveals global length and composition of protein ubiquitylation in cells.","description":"Protein ubiquitylation regulates diverse cellular processes via distinct ubiquitin chains that differ by linkage type and length. However, a comprehensive method for measuring these properties has not been developed. Here we describe a method for assessing the length of substrate-attached polyubiquitin chains, \"ubiquitin chain protection from trypsinization (Ub-ProT).\" Using Ub-ProT, we found that most ubiquitylated substrates in yeast-soluble lysate are attached to chains of up to seven ubiquitin molecules. Inactivation of the ubiquitin-selective chaperone Cdc48 caused a dramatic increase in chain lengths on substrate proteins, suggesting that Cdc48 complex terminates chain elongation by substrate extraction. In mammalian cells, we found that ligand-activated epidermal growth factor recep","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Feb","modification":"2026-05-03T18:07:10.238Z","creation":"2026-04-07T19:32:20.451Z"},"accession":"S-EPMC5802829","cross_references":{"pubmed":["29410401"],"doi":["10.1038/s41467-018-02869-x"]}}