{"doi":"10.1073/pnas.88.2.575","title":"Computer modeling of synapsin I binding to synaptic vesicles and F-actin: implications for regulation of neurotransmitter release.","abstract":"<jats:p>Synapsin I is a neuron-specific phosphoprotein that binds to small synaptic vesicles and actin filaments in a phosphorylation-dependent fashion. It has been hypothesized that dephosphorylated synapsin I inhibits neurotransmitter release either by forming a cage around synaptic vesicles (cage model) or by anchoring them to the F-actin cytoskeleton of the nerve terminal (crosslinking model). Computer modeling was performed with the aim of testing the impact of phosphorylation on the molecular interactions of synapsin I within the nerve terminal. The results of the simulation experiments demonstrate that in the crosslinking model the phosphorylation of synapsin I causes a severalfold increase in the number of vesicles released from the cytoskeleton and that in the cage model the phosphorylation induces a 2-fold increase in the number of vesicles bearing one or more unsaturated synapsin I binding sites. These data are compatible with the view that the function of synapsin I in the short-term regulation of neurotransmitter release is to induce a phosphorylation-dependent transition of synaptic vesicles from a \"reserve pool\" to a readily \"releasable pool\" of vesicles.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1991,"id":674294,"datarank":0.6307038929086449,"base_score":4.204692619390966,"endowment":4.204692619390966,"self_citation_contribution":0.6307038929086449,"citation_network_contribution":0.0,"self_endowment_contribution":0.6307038929086449,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":66,"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":1761741,"name":"F Valtorta","orcid":null,"position":1,"is_corresponding":false},{"id":1528465,"name":"P Greengard","orcid":null,"position":2,"is_corresponding":false},{"id":1761740,"name":"F Benfenati","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Computer modeling of synapsin I binding to synaptic vesicles and F-actin: implications for regulation of neurotransmitter release.","abstract":"<jats:p>Synapsin I is a neuron-specific phosphoprotein that binds to small synaptic vesicles and actin filaments in a phosphorylation-dependent fashion. It has been hypothesized that dephosphorylated synapsin I inhibits neurotransmitter release either by forming a cage around synaptic vesicles (cage model) or by anchoring them to the F-actin cytoskeleton of the nerve terminal (crosslinking model). Computer modeling was performed with the aim of testing the impact of phosphorylation on the molecular interactions of synapsin I within the nerve terminal. The results of the simulation experiments demonstrate that in the crosslinking model the phosphorylation of synapsin I causes a severalfold increase in the number of vesicles released from the cytoskeleton and that in the cage model the phosphorylation induces a 2-fold increase in the number of vesicles bearing one or more unsaturated synapsin I binding sites. These data are compatible with the view that the function of synapsin I in the short-term regulation of neurotransmitter release is to induce a phosphorylation-dependent transition of synaptic vesicles from a \"reserve pool\" to a readily \"releasable pool\" of vesicles.</jats:p>","is_dataset_classified":null,"base_score":4.204692619390966,"endowment":4.204692619390966,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"1671174","pmcid":"PMC50854","openalex_id":"https://openalex.org/W1979610937","authors":[],"funders":[{"funder_name":"NIMH NIH HHS","grant_id":"MH39327","title":null}],"total_grants":1,"fwci":3.3076,"citation_percentile":0.94330026,"influential_citations":0,"citation_trend":[{"year":2014,"count":1},{"year":2015,"count":1},{"year":2017,"count":2},{"year":2018,"count":2},{"year":2021,"count":2},{"year":2025,"count":1}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/50854","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/50854","host_type":"repository"},{"url":"https://pnas.org/doi/pdf/10.1073/pnas.88.2.575","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.88.2.575","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/1671174","host_type":"repository"},{"url":"http://hdl.handle.net/11567/331448","host_type":"repository"}],"fields_of_study":["Photoreceptor and optogenetics research","Lipid Membrane Structure and Behavior","Cellular transport and secretion","Actins","Animals","Computer Simulation","Kinetics","Mathematics","Models, Neurological","Nerve Tissue Proteins","Neurotransmitter Agents","Phosphoproteins","Protein Binding","Synapsins","Synaptic Vesicles"],"mesh_terms":["Actins","Animals","Computer Simulation","Kinetics","Mathematics","Models, Neurological","Nerve Tissue Proteins","Phosphoproteins","Protein Binding","Synaptic Vesicles","Synapsins","Neurotransmitter Agents"],"keywords":["Synapsin","Synapsin I","Synaptic vesicle","Neurotransmitter","Phosphoprotein","Phosphorylation","Cell biology","Vesicle","Neurotransmission","Biology","Biophysics","Chemistry","Biochemistry","Membrane","Receptor"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T16:21:45.353013Z","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":[]}