{"doi":"10.1038/s42003-024-07172-8","title":"N-terminal cleavage of cyclophilin D boosts its ability to bind F-ATP synthase","abstract":null,"journal":"Communications Biology","year":2024,"id":610037,"datarank":0.3596842909197557,"base_score":2.3978952727983707,"endowment":2.3978952727983707,"self_citation_contribution":0.3596842909197557,"citation_network_contribution":0.0,"self_endowment_contribution":0.3596842909197557,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":10,"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":1568252,"name":"Alessandro Negro","orcid":null,"position":1,"is_corresponding":false},{"id":1568253,"name":"Antonio Filippi","orcid":null,"position":2,"is_corresponding":false},{"id":1568254,"name":"Camilla Bean","orcid":null,"position":3,"is_corresponding":false},{"id":1568255,"name":"Valentina Pia Muraca","orcid":null,"position":4,"is_corresponding":false},{"id":1568256,"name":"Clarissa Gissi","orcid":null,"position":5,"is_corresponding":false},{"id":1156739,"name":"Diana Canetti","orcid":"0000-0001-5292-8124","position":6,"is_corresponding":false},{"id":1156738,"name":"Maria Chiara Mimmi","orcid":"0000-0002-5165-9230","position":7,"is_corresponding":false},{"id":1568257,"name":"Elisa Zamprogno","orcid":null,"position":8,"is_corresponding":false},{"id":1568258,"name":"Francesco Ciscato","orcid":null,"position":9,"is_corresponding":false},{"id":1568259,"name":"Laura Acquasaliente","orcid":"0000-0001-6495-0871","position":10,"is_corresponding":false},{"id":467801,"name":"Vincenzo De Filippis","orcid":"0000-0001-9775-8894","position":11,"is_corresponding":false},{"id":1568260,"name":"Marina Comelli","orcid":null,"position":12,"is_corresponding":false},{"id":1261091,"name":"Michela Carraro","orcid":"0000-0002-4573-9306","position":13,"is_corresponding":false},{"id":1568261,"name":"Andrea Rasola","orcid":"0000-0003-4522-3008","position":14,"is_corresponding":false},{"id":1014103,"name":"Christoph Gerle","orcid":"0000-0002-7265-2804","position":15,"is_corresponding":false},{"id":542901,"name":"Paolo Bernardi","orcid":"0000-0001-9187-3736","position":16,"is_corresponding":false},{"id":1568262,"name":"Alessandra Corazza","orcid":"0000-0003-2272-1928","position":17,"is_corresponding":false},{"id":1568263,"name":"Giovanna Lippe","orcid":"0000-0003-0042-5052","position":18,"is_corresponding":false},{"id":1568251,"name":"Gabriele Coluccino","orcid":"0009-0007-9173-7807","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"N-terminal cleavage of cyclophilin D boosts its ability to bind F-ATP synthase.","abstract":"Cyclophilin (CyP) D is a regulator of the mitochondrial F-ATP synthase. Here we report the discovery of a form of CyPD lacking the first 10 (mouse) or 13 (human) N-terminal residues (ΔN-CyPD), a protein region with species-specific features. NMR studies on recombinant human full-length CyPD (FL-CyPD) and ΔN-CyPD form revealed that the N-terminus is highly flexible, in contrast with the rigid globular part. We have studied the interactions of FL and ΔN-CyPD with F-ATP synthase at the OSCP subunit, a site where CyPD binding inhibits catalysis and favors the transition of the enzyme complex to the permeability transition pore. At variance from FL-CyPD, ΔN-CyPD binds OSCP in saline media, indicating that the N-terminus substantially decreases the binding affinity for OSCP. We also provide evidence that calpain 1 is responsible for generation of ΔN-CyPD in cells. Altogether, our work suggests the existence of a novel mechanism of modulation of CyPD through cleavage of its N-terminus that may have significant pathophysiological implications.","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":"39528709","pmcid":"PMC11555324","openalex_id":null,"authors":[],"funders":[{"funder_name":"Ministero dell'Istruzione, dell'Università e della Ricerca (Ministry of Education, University and Research)","grant_id":"LHFW42","title":null},{"funder_name":"Ministero dell'Istruzione dell'Università e della Ricerca","grant_id":"unidentified","title":"unidentified"},{"funder_name":"Università degli Studi di Udine","grant_id":"","title":null}],"total_grants":3,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"gold","license":"cc-by-nc-nd","oa_locations":[{"url":"https://www.nature.com/articles/s42003-024-07172-8.pdf","host_type":"publisher"},{"url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC11555324/pdf/42003_2024_Article_7172.pdf","host_type":"repository"},{"url":"https://europepmc.org/articles/PMC11555324","host_type":"Europe_PMC"},{"url":"https://europepmc.org/articles/PMC11555324?pdf=render","host_type":"Europe_PMC"},{"url":"https://doi.org/10.1038/s42003-024-07172-8","host_type":""},{"url":"https://pubmed.ncbi.nlm.nih.gov/39528709","host_type":""},{"url":"http://dx.doi.org/10.1038/s42003-024-07172-8","host_type":""},{"url":"https://doaj.org/article/396ffbc5f7dc47788870300bd1a4f6a6","host_type":""},{"url":"https://hdl.handle.net/20.500.14243/539654","host_type":""},{"url":"https://hdl.handle.net/11577/3541534","host_type":""},{"url":"https://hdl.handle.net/11390/1294386","host_type":""}],"fields_of_study":["0301 basic medicine","0303 health sciences","03 medical and health sciences"],"mesh_terms":["Animals","Humans","Mice","Proton-Translocating ATPases","Mitochondrial Proton-Translocating ATPases","Cyclophilins","Protein Binding","Peptidyl-Prolyl Isomerase F","Peptidyl-Prolyl Isomerase D"],"keywords":["CyP D","QH301-705.5","Mitochondrial Proton-Translocating ATPases","F-ATP synthase","Article","Mice","Cyclophilins","Proton-Translocating ATPases","Humans","Peptidyl-Prolyl Isomerase F","Animals","Peptidyl-Prolyl Isomerase D","Biology (General)","Protein Binding"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[{"name":"gen"},{"name":"pdb"},{"name":"doi"}],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-31T18:47:56.962727Z","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":[]}