{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Nahar A"],"funding":["University of Colorado Boulder","National Institutes of Health","NIGMS NIH HHS"],"pagination":["110918"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9214829"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["39(10)"],"pubmed_abstract":["The proteasome holoenzyme regulates the cellular proteome via degrading most proteins. In its 19-subunit regulatory particle (RP), a heterohexameric ATPase enables protein degradation by injecting protein substrates into the core peptidase. RP assembly utilizes \"checkpoints,\" where multiple dedicated chaperones bind to specific ATPase subunits and control the addition of other subunits. Here, we find that the RP assembly checkpoint relies on two common features of the chaperones. Individual chaperones can distinguish an RP, in which their cognate ATPase persists in the ATP-bound state. Chaperones then together modulate ATPase activity to facilitate RP subunit rearrangements for switching to an active, substrate-processing state in the resulting proteasome holoenzyme. Thus, chaperones may s"],"journal":["Cell reports"],"pubmed_title":["Assembly checkpoint of the proteasome regulatory particle is activated by coordinated actions of proteasomal ATPase chaperones."],"pmcid":["PMC9214829"],"funding_grant_id":["R01GM127688","R01 GM127688","R35 GM153336"],"pubmed_authors":["Sekaran S","Nahar A","Orth JD","Park S","Sokolova V"],"additional_accession":[]},"is_claimable":false,"name":"Assembly checkpoint of the proteasome regulatory particle is activated by coordinated actions of proteasomal ATPase chaperones.","description":"The proteasome holoenzyme regulates the cellular proteome via degrading most proteins. In its 19-subunit regulatory particle (RP), a heterohexameric ATPase enables protein degradation by injecting protein substrates into the core peptidase. RP assembly utilizes \"checkpoints,\" where multiple dedicated chaperones bind to specific ATPase subunits and control the addition of other subunits. Here, we find that the RP assembly checkpoint relies on two common features of the chaperones. Individual chaperones can distinguish an RP, in which their cognate ATPase persists in the ATP-bound state. Chaperones then together modulate ATPase activity to facilitate RP subunit rearrangements for switching to an active, substrate-processing state in the resulting proteasome holoenzyme. Thus, chaperones may s","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jun","modification":"2026-05-27T20:28:44.217Z","creation":"2025-02-19T02:43:39.236Z"},"accession":"S-EPMC9214829","cross_references":{"pubmed":["35675778"],"doi":["10.1016/j.celrep.2022.110918"]}}