{"doi":"10.1016/j.bbrc.2006.04.050","title":"The proteasome activator PA28 functions in collaboration with Hsp90 in vivo","abstract":null,"journal":"Biochemical and Biophysical Research Communications","year":2006,"id":640441,"datarank":0.31191623125197543,"base_score":2.0794415416798357,"endowment":2.0794415416798357,"self_citation_contribution":0.31191623125197543,"citation_network_contribution":0.0,"self_endowment_contribution":0.31191623125197543,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":7,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1664440,"name":"Fumika Shinozaki","orcid":null,"position":1,"is_corresponding":false},{"id":1664441,"name":"Miho Suzuki","orcid":null,"position":2,"is_corresponding":false},{"id":1664442,"name":"Katsuhiko Yoshimatsu","orcid":null,"position":3,"is_corresponding":false},{"id":1664443,"name":"Yoshimasa Ichikawa","orcid":null,"position":4,"is_corresponding":false},{"id":1664444,"name":"Yasufumi Minami","orcid":null,"position":5,"is_corresponding":false},{"id":1664439,"name":"Michiko Minami","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"The proteasome activator PA28 functions in collaboration with Hsp90 in vivo","abstract":"We have previously shown that the proteasome activator PA28 is essential to Hsp90-dependent protein refolding in vitro, where PA28 mediates transfer of the Hsp90-bound substrate protein to the Hsc70/Hsp40 chaperone machine for its correct refolding. This observation suggests that PA28 may also collaborate with Hsp90 in cells. To examine this possibility, here we have used double-stranded RNA interference (RNAi) against PA28 in Caenorhabditis elegans mutants of daf-21, which encodes Hsp90. We show that C. elegans PA28 facilitates Hsp90-initiated protein refolding, albeit with an activity lower than that of mouse PA28 proteins. RNAi-mediated knockdown of PA28 significantly suppresses the Daf-c (dauer formation constitutive) phenotype of the daf-21 mutant, but it has no affect on the distinct defects of this mutant in sensing odorants. Taking these results together, we conclude that PA28 is likely to function in collaboration with Hsp90 in vivo.","is_dataset_classified":null,"base_score":2.0794415416798357,"endowment":2.0794415416798357,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"16650828","pmcid":null,"openalex_id":"https://openalex.org/W2016803689","authors":[],"funders":[{"funder_name":"National Institutes of Health","grant_id":"","title":null},{"funder_name":"Ministry of Education, Culture, Sports, Science and Technology","grant_id":"","title":null},{"funder_name":"Japan Health Sciences Foundation","grant_id":"","title":null}],"total_grants":3,"fwci":0.2701,"citation_percentile":0.56682374,"influential_citations":0,"citation_trend":[{"year":2015,"count":1},{"year":2020,"count":1},{"year":2022,"count":1},{"year":2023,"count":1},{"year":2025,"count":1}],"oa_status":"closed","license":"https://www.elsevier.com/legal/tdmrep-license","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S0006291X06009065?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0006291X06009065?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.bbrc.2006.04.050","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/16650828","host_type":"repository"}],"fields_of_study":["Heat shock proteins research","Genetics, Aging, and Longevity in Model Organisms","Spaceflight effects on biology"],"mesh_terms":["Animals","Phenotype","Caenorhabditis elegans","Receptors, Cytoplasmic and Nuclear","HSP90 Heat-Shock Proteins","Caenorhabditis elegans Proteins","RNA Interference","Proteasome Endopeptidase Complex","Proteasome Inhibitors"],"keywords":["Hsp90","RNA interference","Gene knockdown","Caenorhabditis elegans","Activator (genetics)","Mutant","Chaperone (clinical)","Proteasome","Cell biology","In vivo","Phenotype","Chemistry","Biology","Biochemistry","Gene","RNA","Genetics","Heat shock protein"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-07T11:55:08.208926Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}