{"doi":"10.1073/pnas.95.19.11241","title":"Two yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex","abstract":"<jats:p>\n                    We sublocalized the yeast nucleoporin Nup82 to the cytoplasmic side of the nuclear pore complex (NPC) by immunoelectron microscopy. Moreover, by\n                    <jats:italic>in vitro</jats:italic>\n                    binding assays we showed that Nup82 interacts with the C-terminal region of Nup159, a yeast nucleoporin that previously was also localized to the cytoplasmic side of the NPC. Hence, the two nucleoporins, Nup82 and Nup159, form a cytoplasmically oriented subcomplex that is likely to be part of the fibers emanating from the cytoplasmic ring of the NPC. Overexpression of Rss1/Gle1, a putative nucleoporin and/or mRNA transport factor, was shown previously to partially rescue depletion of Nup159. We show here that overexpression of Rss1/Gle1 also partially rescued depletion of Nup82. Depletion of either Nup82, Nup159, or Rss1/Gle1 was shown previously to inhibit mRNA export. As was reported previously for depletion of Nup159 or of Rss1/Gle1, we show here that depletion of Nup82 has no detectable effect on classical nuclear localization sequence-mediated nuclear import. In summary, the nucleoporins Nup159 and Nup82 form a cytoplasmically oriented subcomplex of the NPC that is likely associated with Rss1/Gle1; this complex is essential for RNA export, but not for classical nuclear localization sequence-mediated nuclear protein import.\n                  </jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1998,"id":617338,"datarank":3.302338412619439,"base_score":4.110873864173311,"endowment":4.110873864173311,"self_citation_contribution":0.6166310796259968,"citation_network_contribution":2.685707332993442,"self_endowment_contribution":0.6166310796259968,"citer_contribution":2.685707332993442,"corpus_percentile":null,"corpus_rank":null,"citation_count":60,"citer_count":57,"citers_with_citation_signal":54,"citers_with_endowment":54,"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":1592037,"name":"Caterina Strambio-de-Castillia","orcid":null,"position":1,"is_corresponding":false},{"id":974765,"name":"Günter Blobel","orcid":"0000-0002-7839-8341","position":2,"is_corresponding":false},{"id":854419,"name":"Michael E. Hurwitz","orcid":"0000-0002-1326-7308","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Two yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex","abstract":"<jats:p>\n                    We sublocalized the yeast nucleoporin Nup82 to the cytoplasmic side of the nuclear pore complex (NPC) by immunoelectron microscopy. Moreover, by\n                    <jats:italic>in vitro</jats:italic>\n                    binding assays we showed that Nup82 interacts with the C-terminal region of Nup159, a yeast nucleoporin that previously was also localized to the cytoplasmic side of the NPC. Hence, the two nucleoporins, Nup82 and Nup159, form a cytoplasmically oriented subcomplex that is likely to be part of the fibers emanating from the cytoplasmic ring of the NPC. Overexpression of Rss1/Gle1, a putative nucleoporin and/or mRNA transport factor, was shown previously to partially rescue depletion of Nup159. We show here that overexpression of Rss1/Gle1 also partially rescued depletion of Nup82. Depletion of either Nup82, Nup159, or Rss1/Gle1 was shown previously to inhibit mRNA export. As was reported previously for depletion of Nup159 or of Rss1/Gle1, we show here that depletion of Nup82 has no detectable effect on classical nuclear localization sequence-mediated nuclear import. In summary, the nucleoporins Nup159 and Nup82 form a cytoplasmically oriented subcomplex of the NPC that is likely associated with Rss1/Gle1; this complex is essential for RNA export, but not for classical nuclear localization sequence-mediated nuclear protein import.\n                  </jats:p>","is_dataset_classified":null,"base_score":4.110873864173311,"endowment":4.110873864173311,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"9736720","pmcid":"PMC21626","openalex_id":"https://openalex.org/W1991301196","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"T32 GM007739","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"GM07739","title":null}],"total_grants":2,"fwci":2.4454,"citation_percentile":0.89550235,"influential_citations":0,"citation_trend":[{"year":2012,"count":4},{"year":2013,"count":1},{"year":2014,"count":1},{"year":2016,"count":1},{"year":2017,"count":1},{"year":2020,"count":1},{"year":2021,"count":2},{"year":2022,"count":1}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://pnas.org/doi/pdf/10.1073/pnas.95.19.11241","host_type":"publisher"},{"url":"https://doi.org/10.1073/pnas.95.19.11241","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/9736720","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/21626","host_type":"repository"}],"fields_of_study":["Nuclear Structure and Function","RNA Research and Splicing","Genomics and Chromatin Dynamics","Fungal Proteins","Gene Expression Regulation, Fungal","Membrane Proteins","Microscopy, Immunoelectron","Nuclear Envelope","Nuclear Pore Complex Proteins","Nuclear Proteins","Phenotype","RNA Helicases","RNA, Messenger","Repressor Proteins","Saccharomyces cerevisiae Proteins"],"mesh_terms":["Fungal Proteins","Membrane Proteins","Nuclear Envelope","Nuclear Proteins","Phenotype","Repressor Proteins","RNA, Messenger","Gene Expression Regulation, Fungal","Microscopy, Immunoelectron","RNA Helicases","Nuclear Pore Complex Proteins","Saccharomyces cerevisiae Proteins"],"keywords":["Nucleoporin","Nuclear pore","Immunoelectron microscopy","Cell biology","Nuclear transport","Cytoplasm","Biology","Nuclear protein","Nuclear export signal","RNA-binding protein","Nuclear localization sequence","Messenger RNA","Cell nucleus","Biochemistry","Genetics","Gene","Transcription factor"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-03T01:27:28.511507Z","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":[]}