{"doi":"10.1073/pnas.1401359111","title":"SUMOylation regulates telomere length by targeting the shelterin subunit Tpz1\n                    <sup>Tpp1</sup>\n                    to modulate shelterin–Stn1 interaction in fission yeast","abstract":"<jats:title>Significance</jats:title>\n                  <jats:p>\n                    Telomeres protect DNA ends of linear eukaryotic chromosomes from degradation and fusion through the recruitment of telomerase. We previously found that SUMOylation negatively regulates telomere extension; however, how SUMOylation limits telomere extension has remained unknown until now. Here we provide major mechanistic insights into how the SUMOylation pathway collaborates with shelterin and Stn1-Ten1 complexes to regulate telomere length. We establish that SUMOylation of the shelterin subunit TPP1 homolog in\n                    <jats:italic>Schizosaccharomyces pombe</jats:italic>\n                    (Tpz1) prevents telomerase accumulation at telomeres by promoting recruitment of Stn1-Ten1 to telomeres in S-phase. Thus, our findings establish that Tpz1 not only contributes to telomerase recruitment via its interaction with Ccq1-Est1, but also contributes to the negative regulation of telomerase via its SUMOylation-mediated interaction with Stn1-Ten1.\n                  </jats:p>","journal":"Proceedings of the National Academy of Sciences","year":2014,"id":682236,"datarank":0.6010999777848708,"base_score":4.007333185232471,"endowment":4.007333185232471,"self_citation_contribution":0.6010999777848708,"citation_network_contribution":0.0,"self_endowment_contribution":0.6010999777848708,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":54,"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":1782352,"name":"Ross S. Low","orcid":null,"position":1,"is_corresponding":false},{"id":1782353,"name":"Venny Santosa","orcid":null,"position":2,"is_corresponding":false},{"id":1782354,"name":"Hiroki Tsuji","orcid":null,"position":3,"is_corresponding":false},{"id":1782355,"name":"Bettina A. Moser","orcid":null,"position":4,"is_corresponding":false},{"id":1782356,"name":"Shiho Fujisawa","orcid":null,"position":5,"is_corresponding":false},{"id":1782357,"name":"Jennifer L. Harland","orcid":null,"position":6,"is_corresponding":false},{"id":580982,"name":"Olga N. Raguimova","orcid":null,"position":7,"is_corresponding":false},{"id":1782358,"name":"Andrew Go","orcid":null,"position":8,"is_corresponding":false},{"id":1782359,"name":"Masaru Ueno","orcid":null,"position":9,"is_corresponding":false},{"id":1782360,"name":"Akihisa Matsuyama","orcid":null,"position":10,"is_corresponding":false},{"id":114450,"name":"Minoru Yoshida","orcid":null,"position":11,"is_corresponding":false},{"id":1782361,"name":"Toru M. Nakamura","orcid":null,"position":12,"is_corresponding":false},{"id":1599780,"name":"Katsunori Tanaka","orcid":null,"position":13,"is_corresponding":false},{"id":1782351,"name":"Keisuke Miyagawa","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"SUMOylation regulates telomere length by targeting the shelterin subunit Tpz1\n                    <sup>Tpp1</sup>\n                    to modulate shelterin–Stn1 interaction in fission yeast","abstract":"<jats:title>Significance</jats:title>\n                  <jats:p>\n                    Telomeres protect DNA ends of linear eukaryotic chromosomes from degradation and fusion through the recruitment of telomerase. We previously found that SUMOylation negatively regulates telomere extension; however, how SUMOylation limits telomere extension has remained unknown until now. Here we provide major mechanistic insights into how the SUMOylation pathway collaborates with shelterin and Stn1-Ten1 complexes to regulate telomere length. We establish that SUMOylation of the shelterin subunit TPP1 homolog in\n                    <jats:italic>Schizosaccharomyces pombe</jats:italic>\n                    (Tpz1) prevents telomerase accumulation at telomeres by promoting recruitment of Stn1-Ten1 to telomeres in S-phase. Thus, our findings establish that Tpz1 not only contributes to telomerase recruitment via its interaction with Ccq1-Est1, but also contributes to the negative regulation of telomerase via its SUMOylation-mediated interaction with Stn1-Ten1.\n                  </jats:p>","is_dataset_classified":null,"base_score":4.007333185232471,"endowment":4.007333185232471,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"24711392","pmcid":"PMC4000806","openalex_id":"https://openalex.org/W2093591854","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM078253","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM078253","title":null}],"total_grants":2,"fwci":3.1194,"citation_percentile":0.92511725,"influential_citations":0,"citation_trend":[{"year":2014,"count":2},{"year":2015,"count":7},{"year":2016,"count":7},{"year":2017,"count":8},{"year":2018,"count":5},{"year":2019,"count":3},{"year":2020,"count":1},{"year":2021,"count":1},{"year":2022,"count":3},{"year":2023,"count":16},{"year":2026,"count":1}],"oa_status":"bronze","license":null,"oa_locations":[{"url":"https://www.pnas.org/content/pnas/111/16/5950.full.pdf","host_type":"journal"},{"url":"https://www.pnas.org/content/pnas/111/16/5950.full.pdf","host_type":"publisher"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.1401359111","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.1401359111","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/24711392","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/4000806","host_type":"repository"}],"fields_of_study":["Ubiquitin and proteasome pathways","Telomeres, Telomerase, and Senescence","DNA Repair Mechanisms","Carrier Proteins","DNA-Binding Proteins","G2 Phase","Ligases","Lysine","Models, Biological","Protein Binding","Protein Subunits","S Phase","Schizosaccharomyces","Schizosaccharomyces pombe Proteins","Sumoylation","Telomerase","Telomere","Telomere Homeostasis","Telomere Shortening","Telomere-Binding Proteins","Ubiquitin-Protein Ligases"],"mesh_terms":["Carrier Proteins","DNA-Binding Proteins","Ligases","Lysine","Models, Biological","Protein Binding","Schizosaccharomyces","G2 Phase","S Phase","Telomere","Telomerase","Protein Subunits","Schizosaccharomyces pombe Proteins","Telomere-Binding Proteins","Ubiquitin-Protein Ligases","Sumoylation","Telomere Homeostasis","Telomere Shortening"],"keywords":["Shelterin","SUMO protein","Telomere","Telomerase","Schizosaccharomyces","Schizosaccharomyces pombe","Biology","Telomere-binding protein","Cell biology","Protein subunit","Genetics","Ubiquitin","DNA","Saccharomyces cerevisiae","DNA-binding protein","Yeast","Transcription factor","Cell cycle","DNA replication","S-phase","Cst Complex"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life in Land"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-17T19:49:23.557364Z","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":[]}