{"doi":"10.1016/j.bbamcr.2013.02.005","title":"PTPA activates protein phosphatase-2A through reducing its phosphorylation at tyrosine-307 with upregulation of protein tyrosine phosphatase 1B","abstract":null,"journal":"Biochimica et Biophysica Acta (BBA) - Molecular Cell Research","year":2013,"id":665356,"datarank":0.5333022092234121,"base_score":3.5553480614894135,"endowment":3.5553480614894135,"self_citation_contribution":0.5333022092234121,"citation_network_contribution":0.0,"self_endowment_contribution":0.5333022092234121,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":34,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":2,"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":1737442,"name":"Yun-Juan Nie","orcid":null,"position":1,"is_corresponding":false},{"id":1737443,"name":"Hai-Rong Shi","orcid":null,"position":2,"is_corresponding":false},{"id":1737444,"name":"Zhong-Fei Ni","orcid":null,"position":3,"is_corresponding":false},{"id":824244,"name":"Qun Wang","orcid":"0000-0003-4853-1727","position":4,"is_corresponding":false},{"id":1511653,"name":"Jian-Zhi Wang","orcid":null,"position":5,"is_corresponding":false},{"id":1737445,"name":"Gong-Ping Liu","orcid":null,"position":6,"is_corresponding":false},{"id":546659,"name":"Yu Luo","orcid":"0000-0002-7939-5505","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"PTPA activates protein phosphatase-2A through reducing its phosphorylation at tyrosine-307 with upregulation of protein tyrosine phosphatase 1B","abstract":"Protein phosphatase-2A (PP2A), an important phosphatase in dephosphorylating tau and preserving synapse, is significantly suppressed in Alzheimer's disease (AD), but the mechanism is not well understood. Here, we studied whether phosphotyrosyl phosphatase activator (PTPA) could activate PP2A by reducing its inhibitory phosphorylation at tyrosine 307 (P-PP2AC). We found that overexpression of PTPA activated PP2A by decreasing the level of P-PP2AC with reduced phosphorylation of tau, while knockdown of PTPA inhibited PP2A by increasing the level of P-PP2AC with enhanced tau phosphorylation. We also observed that expression of PTPA could upregulate the protein and mRNA levels of protein tyrosine phosphatase 1B (PTP1B) and simultaneous downregulation of PTP1B eliminated PTPA-induced PP2A activation. Importantly, we also found that the protein level of PTPA is downregulated in the brains of AD patients, and the AD transgenic mouse models with expression of mutant human amyloid precursor protein (hAPP) or the longest human tau (htau), respectively. Our data indicate that PTPA may activate PP2A through activating PTP1B and thus reducing the level of P-PP2AC, therefore upregulation of PTPA may represent a potential strategy in rescuing PP2A and arresting tau pathology in AD.","is_dataset_classified":null,"base_score":3.5553480614894135,"endowment":3.5553480614894135,"datacite_reuse_total":2,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"23428800","pmcid":null,"openalex_id":"https://openalex.org/W2078377364","authors":[],"funders":[{"funder_name":"National Natural Science Foundation of China","grant_id":"30801212","title":null}],"total_grants":1,"fwci":0.6869,"citation_percentile":0.72580877,"influential_citations":0,"citation_trend":[{"year":2014,"count":4},{"year":2016,"count":2},{"year":2017,"count":3},{"year":2018,"count":4},{"year":2019,"count":6},{"year":2020,"count":4},{"year":2021,"count":4},{"year":2022,"count":1},{"year":2023,"count":4},{"year":2024,"count":1},{"year":2025,"count":1}],"oa_status":"closed","license":"https://www.elsevier.com/open-access/userlicense/1.0/","oa_locations":[{"url":"https://api.elsevier.com/content/article/PII:S0167488913000529?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0167488913000529?httpAccept=text/plain","host_type":"publisher"},{"url":"https://doi.org/10.1016/j.bbamcr.2013.02.005","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/23428800","host_type":"repository"},{"url":"http://ir.lzu.edu.cn/handle/262010/190582","host_type":"repository"}],"fields_of_study":["MicroRNA in disease regulation","Protein Tyrosine Phosphatases","ATP Synthase and ATPases Research","Alzheimer Disease","Amyloid beta-Protein Precursor","Animals","Brain","Down-Regulation","Humans","Mice","Mice, Transgenic","Neurons","Phosphoprotein Phosphatases","Phosphorylation","Protein Phosphatase 2","Protein Tyrosine Phosphatase, Non-Receptor Type 1","Tyrosine","Up-Regulation","tau Proteins"],"mesh_terms":["Alzheimer Disease","Animals","Brain","Humans","Mice, Transgenic","Neurons","Phosphoprotein Phosphatases","Phosphorylation","Tyrosine","Down-Regulation","Up-Regulation","Amyloid beta-Protein Precursor","tau Proteins","Mice","Protein Tyrosine Phosphatase, Non-Receptor Type 1","Protein Phosphatase 2"],"keywords":["Protein phosphatase 2","Protein tyrosine phosphatase","Downregulation and upregulation","Phosphorylation","Phosphatase","Tyrosine phosphorylation","Tyrosine","Cell biology","Chemistry","Immunoprecipitation","Gene knockdown","DUSP6","Biology","Biochemistry","Gene"],"sdg_mappings":[],"linked_datasets":[{"doi":"10.6084/m9.figshare.22617823.v1","title":"Additional file 1 of Aqueous extract of Platycodon grandiflorus attenuates lipopolysaccharide-induced apoptosis and inflammatory cell infiltration in mouse lungs by inhibiting PI3K/Akt signaling","publisher":"figshare","resource_type":"JournalArticle"},{"doi":"10.6084/m9.figshare.22617823","title":"Additional file 1 of Aqueous extract of Platycodon grandiflorus attenuates lipopolysaccharide-induced apoptosis and inflammatory cell infiltration in mouse lungs by inhibiting PI3K/Akt signaling","publisher":"figshare","resource_type":"JournalArticle"}],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-13T08:28:17.564230Z","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":[]}