{"doi":"10.1128/jvi.80.4.1798-1806.2006","title":"Importin-β Family Members Mediate Alpharetrovirus Gag Nuclear Entry via Interactions with Matrix and Nucleocapsid","abstract":"<jats:title>ABSTRACT</jats:title>\n          <jats:p>\n            The retroviral Gag polyprotein orchestrates the assembly and release of virus particles from infected cells. We previously reported that nuclear transport of the Rous sarcoma virus (RSV) Gag protein is intrinsic to the virus assembly pathway. To identify\n            <jats:italic>cis-</jats:italic>\n            and\n            <jats:italic>trans-</jats:italic>\n            acting factors governing nucleocytoplasmic trafficking, we developed novel vectors to express regions of Gag in\n            <jats:italic>Saccharomyces cerevisiae</jats:italic>\n            . The localization of Gag proteins was examined in the wild type and in mutant strains deficient in members of the importin-β family. We confirmed the Crm1p dependence of the previously identified Gag p10 nuclear export signal. The known nuclear localization signal (NLS) in MA (matrix) was also functional in\n            <jats:italic>S. cerevisiae</jats:italic>\n            , and additionally we discovered a novel NLS within the NC (nucleocapsid) domain of Gag. MA utilizes Kap120p and Mtr10p import receptors while nuclear entry of NC involves the classical importin-α/β (Kap60p/95p) pathway. NC also possesses nuclear targeting activity in avian cells and contains the primary signal for the import of the Gag polyprotein. Thus, the nucleocytoplasmic dynamics of RSV Gag depend upon the counterbalance of Crm1p-mediated export with two independent NLSs, each interacting with distinct nuclear import factors.\n          </jats:p>","journal":"Journal of Virology","year":2006,"id":643843,"datarank":0.6238324625039509,"base_score":4.1588830833596715,"endowment":4.1588830833596715,"self_citation_contribution":0.6238324625039509,"citation_network_contribution":0.0,"self_endowment_contribution":0.6238324625039509,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":63,"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":1049488,"name":"Lisa Z. Scheifele","orcid":"0000-0003-1400-6895","position":1,"is_corresponding":false},{"id":161487,"name":"Eileen P. Ryan","orcid":null,"position":2,"is_corresponding":false},{"id":367378,"name":"Anita K. Hopper","orcid":"0000-0002-7884-2932","position":3,"is_corresponding":false},{"id":392116,"name":"Leslie J. Parent","orcid":"0000-0002-0431-9049","position":4,"is_corresponding":false},{"id":1675478,"name":"Kristin L. Butterfield-Gerson","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Importin-β Family Members Mediate Alpharetrovirus Gag Nuclear Entry via Interactions with Matrix and Nucleocapsid","abstract":"<jats:title>ABSTRACT</jats:title>\n          <jats:p>\n            The retroviral Gag polyprotein orchestrates the assembly and release of virus particles from infected cells. We previously reported that nuclear transport of the Rous sarcoma virus (RSV) Gag protein is intrinsic to the virus assembly pathway. To identify\n            <jats:italic>cis-</jats:italic>\n            and\n            <jats:italic>trans-</jats:italic>\n            acting factors governing nucleocytoplasmic trafficking, we developed novel vectors to express regions of Gag in\n            <jats:italic>Saccharomyces cerevisiae</jats:italic>\n            . The localization of Gag proteins was examined in the wild type and in mutant strains deficient in members of the importin-β family. We confirmed the Crm1p dependence of the previously identified Gag p10 nuclear export signal. The known nuclear localization signal (NLS) in MA (matrix) was also functional in\n            <jats:italic>S. cerevisiae</jats:italic>\n            , and additionally we discovered a novel NLS within the NC (nucleocapsid) domain of Gag. MA utilizes Kap120p and Mtr10p import receptors while nuclear entry of NC involves the classical importin-α/β (Kap60p/95p) pathway. NC also possesses nuclear targeting activity in avian cells and contains the primary signal for the import of the Gag polyprotein. Thus, the nucleocytoplasmic dynamics of RSV Gag depend upon the counterbalance of Crm1p-mediated export with two independent NLSs, each interacting with distinct nuclear import factors.\n          </jats:p>","is_dataset_classified":null,"base_score":4.1588830833596715,"endowment":4.1588830833596715,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"16439536","pmcid":"PMC1367160","openalex_id":"https://openalex.org/W2136220110","authors":[],"funders":[{"funder_name":"NCI NIH HHS","grant_id":"R01 CA076534","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM027930","title":null},{"funder_name":"NCI NIH HHS","grant_id":"R01CA76534","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01GM27930","title":null}],"total_grants":4,"fwci":1.7807,"citation_percentile":0.83744787,"influential_citations":0,"citation_trend":[{"year":2012,"count":8},{"year":2013,"count":3},{"year":2014,"count":1},{"year":2015,"count":2},{"year":2016,"count":3},{"year":2018,"count":1},{"year":2020,"count":6},{"year":2021,"count":3},{"year":2022,"count":1},{"year":2023,"count":4},{"year":2024,"count":3},{"year":2025,"count":4}],"oa_status":"green","license":"https://journals.asm.org/non-commercial-tdm-license","oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/1367160","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/1367160","host_type":"repository"},{"url":"https://journals.asm.org/doi/pdf/10.1128/JVI.80.4.1798-1806.2006","host_type":"publisher"},{"url":"https://doi.org/10.1128/jvi.80.4.1798-1806.2006","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/16439536","host_type":"repository"}],"fields_of_study":["Nuclear Structure and Function","RNA Research and Splicing","Virus-based gene therapy research","Avian Sarcoma Viruses","Gene Deletion","Gene Products, gag","Genetic Vectors","Karyopherins","Microscopy, Confocal","Mutation","Nuclear Localization Signals","Nucleocapsid","Nucleocytoplasmic Transport Proteins","Protein Binding","Protein Transport","RNA-Binding Proteins","Receptors, Cytoplasmic and Nuclear","Saccharomyces cerevisiae","Saccharomyces cerevisiae Proteins","Viral Matrix Proteins","beta Karyopherins","Exportin 1 Protein"],"mesh_terms":["Exportin 1 Protein","Avian Sarcoma Viruses","Genetic Vectors","Mutation","Protein Binding","Saccharomyces cerevisiae","Viral Matrix Proteins","Gene Products, gag","RNA-Binding Proteins","Gene Deletion","Receptors, Cytoplasmic and Nuclear","Microscopy, Confocal","Nucleocapsid","Nuclear Localization Signals","Protein Transport","Karyopherins","beta Karyopherins","Nucleocytoplasmic Transport Proteins","Saccharomyces cerevisiae Proteins"],"keywords":["Nuclear transport","Importin","NLS","Nuclear localization sequence","Biology","Group-specific antigen","Rous sarcoma virus","Cell biology","Nuclear export signal","Saccharomyces cerevisiae","Capsid","Mutant","Viral matrix protein","Cell nucleus","Virology","Virus","Genetics","Nucleus","Gene"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Partnerships for the goals"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-08T19:14:38.611153Z","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":[]}