{"doi":"10.1371/journal.pone.0145226","title":"Protein Phosphatase Methyl-Esterase PME-1 Protects Protein Phosphatase 2A from Ubiquitin/Proteasome Degradation","abstract":null,"journal":"PLOS ONE","year":2015,"id":596067,"datarank":0.5456379239589579,"base_score":3.6375861597263857,"endowment":3.6375861597263857,"self_citation_contribution":0.5456379239589579,"citation_network_contribution":0.0,"self_endowment_contribution":0.5456379239589579,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":37,"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":1111249,"name":"Akane Miura","orcid":null,"position":1,"is_corresponding":false},{"id":123827,"name":"Tatsuya Usui","orcid":null,"position":2,"is_corresponding":false},{"id":1072328,"name":"Ingrid Mudrak","orcid":null,"position":3,"is_corresponding":false},{"id":139946,"name":"Egon Ogris","orcid":null,"position":4,"is_corresponding":false},{"id":1526538,"name":"Takashi Ohama","orcid":null,"position":5,"is_corresponding":false},{"id":112562,"name":"Koichi Sato","orcid":null,"position":6,"is_corresponding":false},{"id":1526537,"name":"Ryotaro Yabe","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Protein Phosphatase Methyl-Esterase PME-1 Protects Protein Phosphatase 2A from Ubiquitin/Proteasome Degradation","abstract":"Protein phosphatase 2A (PP2A) is a conserved essential enzyme that is implicated as a tumor suppressor based on its central role in phosphorylation-dependent signaling pathways. Protein phosphatase methyl esterase (PME-1) catalyzes specifically the demethylation of the C-terminal Leu309 residue of PP2A catalytic subunit (PP2Ac). It has been shown that PME-1 affects the activity of PP2A by demethylating PP2Ac, but also by directly binding to the phosphatase active site, suggesting loss of PME-1 in cells would enhance PP2A activity. However, here we show that PME-1 knockout mouse embryonic fibroblasts (MEFs) exhibit lower PP2A activity than wild type MEFs. Loss of PME-1 enhanced poly-ubiquitination of PP2Ac and shortened the half-life of PP2Ac protein resulting in reduced PP2Ac levels. Chemical inhibition of PME-1 and rescue experiments with wild type and mutated PME-1 revealed methyl-esterase activity was necessary to maintain PP2Ac protein levels. Our data demonstrate that PME-1 methyl-esterase activity protects PP2Ac from ubiquitin/proteasome degradation.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"26678046","pmcid":"PMC4683032","openalex_id":null,"authors":[],"funders":[],"total_grants":0,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"gold","license":"cc-by","oa_locations":[{"url":"https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0145226&type=printable","host_type":"publisher"},{"url":"http://dx.plos.org/10.1371/journal.pone.0145226","host_type":"publisher"},{"url":"https://doaj.org/article/b9e1f577414e4c8a9b168a027e3190a8","host_type":"repository"},{"url":"https://figshare.com/articles/dataset/_Protein_Phosphatase_Methyl_Esterase_PME_1_Protects_Protein_Phosphatase_2A_from_Ubiquitin_Proteasome_Degradation_/1626414","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/4683032","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC4683032","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC4683032?pdf=render","host_type":"Europe_PMC"}],"fields_of_study":["Animals","Carboxylic Ester Hydrolases","Immunoblotting","Immunoprecipitation","Mice","Mice, Knockout","Proteasome Endopeptidase Complex","Protein Phosphatase 2","Proteolysis","Real-Time Polymerase Chain Reaction","Ubiquitin"],"mesh_terms":["Animals","Mice, Knockout","Mice","Proteasome Endopeptidase Complex","Carboxylic Ester Hydrolases","Ubiquitin","Immunoblotting","Immunoprecipitation","Protein Phosphatase 2","Real-Time Polymerase Chain Reaction","Proteolysis"],"keywords":[],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-27T21:38:45.175252Z","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":[]}