{"doi":"10.1074/jbc.c100228200","title":"Critical Role of WW Domain Phosphorylation in Regulating Phosphoserine Binding Activity and Pin1 Function","abstract":null,"journal":"Journal of Biological Chemistry","year":2002,"id":605183,"datarank":0.8294143631267137,"base_score":5.529429087511423,"endowment":5.529429087511423,"self_citation_contribution":0.8294143631267137,"citation_network_contribution":0.0,"self_endowment_contribution":0.8294143631267137,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":251,"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":292460,"name":"Xiao Zhen Zhou","orcid":"0000-0001-9309-5659","position":1,"is_corresponding":false},{"id":1553085,"name":"Yih-Cherng Liou","orcid":null,"position":2,"is_corresponding":false},{"id":295591,"name":"Joseph P. Noel","orcid":"0000-0002-1277-0331","position":3,"is_corresponding":false},{"id":292461,"name":"Kun Ping Lu","orcid":"0000-0002-0734-1567","position":4,"is_corresponding":false},{"id":1553084,"name":"Pei-Jung Lu","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Critical Role of WW Domain Phosphorylation in Regulating Phosphoserine Binding Activity and Pin1 Function","abstract":"Phosphoserine-binding modules help determine the specificity of signal transduction events. One such module, the group IV WW domain, plays an essential role in targeting the phosphorylation-specific prolyl isomerase Pin1 to its substrates. These modules require Ser/Thr phosphorylation of their ligands for binding activity. However, phosphorylation of these modules and its functional significance have not been described, nor is it known whether the function of Pin1 is regulated. Here we show that Pin1 WW domain is phosphorylated on Ser(16) both in vitro and in vivo. Further, this phosphorylation regulates the ability of the WW domain to mediate Pin1 substrate interaction and cellular localization. Moreover, both Pin1 and WW domain mutants refractory to Ser(16) phosphorylation act as dominant-negative mutants to induce mitotic block and apoptosis and increase multinucleated cells with 8 N DNA content. Thus, phosphorylation is a new mechanism critical for regulating WW domain phosphoserine binding activity and Pin1 function.","is_dataset_classified":null,"base_score":5.529429087511423,"endowment":5.529429087511423,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"11723108","pmcid":null,"openalex_id":"https://openalex.org/W1971696898","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"R01GM56230","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"GM58556","title":null}],"total_grants":2,"fwci":3.5005,"citation_percentile":0.93279639,"influential_citations":0,"citation_trend":[{"year":2012,"count":20},{"year":2013,"count":16},{"year":2014,"count":13},{"year":2015,"count":17},{"year":2016,"count":10},{"year":2017,"count":2},{"year":2018,"count":7},{"year":2019,"count":4},{"year":2020,"count":11},{"year":2021,"count":3},{"year":2022,"count":6},{"year":2023,"count":6},{"year":2024,"count":22},{"year":2025,"count":1},{"year":2026,"count":1}],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"https://doi.org/10.1074/jbc.c100228200","host_type":"journal"},{"url":"https://doi.org/10.1074/jbc.c100228200","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820876819?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925820876819?httpAccept=text/plain","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1074/jbc.C100228200","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/11723108","host_type":"repository"},{"url":"http://www.jbc.org/content/277/4/2381.full.pdf","host_type":"Unpaywall"}],"fields_of_study":["Signaling Pathways in Disease","Peptidase Inhibition and Analysis","Galectins and Cancer Biology","Cell Cycle","DNA","Electrophoresis, Polyacrylamide Gel","Glutathione Transferase","Green Fluorescent Proteins","HeLa Cells","Humans","Luminescent Proteins","Microscopy, Fluorescence","Mitosis","Mutation","NIMA-Interacting Peptidylprolyl Isomerase","Peptidylprolyl Isomerase","Phosphorylation","Phosphoserine","Protein Binding","Protein Structure, Tertiary","Recombinant Fusion Proteins","Serine","Signal Transduction","Threonine","Time Factors"],"mesh_terms":["NIMA-Interacting Peptidylprolyl Isomerase","Cell Cycle","DNA","Electrophoresis, Polyacrylamide Gel","Glutathione Transferase","HeLa Cells","Humans","Luminescent Proteins","Microscopy, Fluorescence","Mitosis","Mutation","Phosphorylation","Phosphoserine","Protein Binding","Recombinant Fusion Proteins","Serine","Threonine","Time Factors","Signal Transduction","Protein Structure, Tertiary","Peptidylprolyl Isomerase","Green Fluorescent Proteins","Hela Cells"],"keywords":["PIN1","Phosphorylation","WW domain","Phosphoserine","Prolyl isomerase","Peptidylprolyl isomerase","Phosphorylation cascade","Cell biology","Biology","Mutant","Signal transduction","Protein phosphorylation","Biochemistry","Serine","Isomerase","Protein kinase A"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-30T01:50:34.912452Z","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":[]}