{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Dao TP"],"funding":["NIGMS NIH HHS","NIH HHS"],"pubmed_abstract":["Highly homologous ubiquitin-binding shuttle proteins UBQLN1, UBQLN2 and UBQLN4 differ in both their specific protein quality control functions and their propensities to localize to stress-induced condensates, cellular aggregates and aggresomes. We previously showed that UBQLN2 phase separates <i>in vitro</i>, and that the phase separation propensities of UBQLN2 deletion constructs correlate with their ability to form condensates in cells. Here, we demonstrated that full-length UBQLN1, UBQLN2 and UBQLN4 exhibit distinct phase behaviors <i>in vitro</i>. Strikingly, UBQLN4 phase separates at a much lower saturation concentration than UBQLN1. However, neither UBQLN1 nor UBQLN4 phase separates with a strong temperature dependence, unlike UBQLN2. We determined that the temperature-dependent phas"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2023.09.27.559790"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10557701"],"repository":["biostudies-literature"],"pubmed_title":["Short N-terminal disordered regions and the proline-rich domain are major regulators of phase transitions for full-length UBQLN1, UBQLN2 and UBQLN4."],"pmcid":["PMC10557701"],"funding_grant_id":["P30 GM138395","R01 GM136946","S10 OD018090"],"pubmed_authors":["Castaneda CA","Haws W","Rajendran A","Galagedera SKK","Dao TP"],"additional_accession":[]},"is_claimable":false,"name":"Short N-terminal disordered regions and the proline-rich domain are major regulators of phase transitions for full-length UBQLN1, UBQLN2 and UBQLN4.","description":"Highly homologous ubiquitin-binding shuttle proteins UBQLN1, UBQLN2 and UBQLN4 differ in both their specific protein quality control functions and their propensities to localize to stress-induced condensates, cellular aggregates and aggresomes. We previously showed that UBQLN2 phase separates <i>in vitro</i>, and that the phase separation propensities of UBQLN2 deletion constructs correlate with their ability to form condensates in cells. Here, we demonstrated that full-length UBQLN1, UBQLN2 and UBQLN4 exhibit distinct phase behaviors <i>in vitro</i>. Strikingly, UBQLN4 phase separates at a much lower saturation concentration than UBQLN1. However, neither UBQLN1 nor UBQLN4 phase separates with a strong temperature dependence, unlike UBQLN2. We determined that the temperature-dependent phas","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Sep","modification":"2025-04-04T09:42:22.155Z","creation":"2025-04-04T09:42:22.155Z"},"accession":"S-EPMC10557701","cross_references":{"pubmed":["37808720"],"doi":["10.1101/2023.09.27.559790"]}}