{"doi":"10.1111/tra.12060","title":"Silencing of Mammalian Sar1 Isoforms Reveals\n                    <scp>COPII</scp>\n                    ‐Independent Protein Sorting and Transport","abstract":"<jats:p>\n                    <jats:bold>\n                      The Sar1\n                      <jats:styled-content style=\"fixed-case\">GTPase</jats:styled-content>\n                      coordinates the assembly of coat protein complex‐\n                      <jats:styled-content style=\"fixed-case\">II</jats:styled-content>\n                      (\n                      <jats:styled-content style=\"fixed-case\">COPII</jats:styled-content>\n                      ) at specific sites of the endoplasmic reticulum (\n                      <jats:styled-content style=\"fixed-case\">ER</jats:styled-content>\n                      ).\n                      <jats:styled-content style=\"fixed-case\">COPII</jats:styled-content>\n                      is required for\n                      <jats:styled-content style=\"fixed-case\">ER</jats:styled-content>\n                      ‐to‐Golgi transport, as it provides a structural and functional framework to ship out protein cargoes produced in the\n                      <jats:styled-content style=\"fixed-case\">ER</jats:styled-content>\n                      . To investigate the requirement of\n                      <jats:styled-content style=\"fixed-case\">COPII</jats:styled-content>\n                      ‐mediated transport in mammalian cells, we used small interfering\n                      <jats:styled-content style=\"fixed-case\">RNA</jats:styled-content>\n                      (\n                      <jats:styled-content style=\"fixed-case\">siRNA</jats:styled-content>\n                      )‐mediated depletion of\n                      <jats:styled-content style=\"fixed-case\">Sar1A</jats:styled-content>\n                      and\n                      <jats:styled-content style=\"fixed-case\">Sar1B</jats:styled-content>\n                      . We report that depletion of these two mammalian forms of Sar1 disrupts\n                      <jats:styled-content style=\"fixed-case\">COPII</jats:styled-content>\n                      assembly and the cells fail to organize transitional elements that coordinate classical\n                      <jats:styled-content style=\"fixed-case\">ER</jats:styled-content>\n                      ‐to‐Golgi protein transfer. Under these conditions, minimal Golgi stacks are seen in proximity to juxtanuclear\n                      <jats:styled-content style=\"fixed-case\">ER</jats:styled-content>\n                      membranes that contain elements of the intermediate compartment, and from which these stacks coordinate biosynthetic transport of protein cargo, such as the vesicular stomatitis virus G protein and albumin. Here, transport of procollagen‐I is inhibited. These data provide proof‐of‐principle for the contribution of alternative mechanisms that support biosynthetic trafficking in mammalian cells, providing evidence of a functional boundary associated with a bypass of\n                      <jats:styled-content style=\"fixed-case\">COPII</jats:styled-content>\n                    </jats:bold>\n                    .\n                  </jats:p>","journal":"Traffic","year":2013,"id":47168,"datarank":2.17975727752443,"base_score":4.204692619390966,"endowment":4.204692619390966,"self_citation_contribution":0.6307038929086449,"citation_network_contribution":1.549053384615785,"self_endowment_contribution":0.6307038929086449,"citer_contribution":1.549053384615785,"corpus_percentile":null,"corpus_rank":null,"citation_count":66,"citer_count":49,"citers_with_citation_signal":45,"citers_with_endowment":45,"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":168533,"name":"Galina V. Beznoussenko","orcid":null,"position":1,"is_corresponding":false},{"id":217715,"name":"Aurora Fusella","orcid":null,"position":2,"is_corresponding":false},{"id":217716,"name":"Oliviano Martella","orcid":null,"position":3,"is_corresponding":false},{"id":217717,"name":"Pedro Moral","orcid":null,"position":4,"is_corresponding":false},{"id":168528,"name":"Alexander A. Mironov","orcid":null,"position":5,"is_corresponding":false},{"id":217714,"name":"Meritxell B. Cutrona","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Silencing of Mammalian Sar1 Isoforms Reveals\n                    <scp>COPII</scp>\n                    ‐Independent Protein Sorting and Transport","abstract":"<jats:p>\n                    <jats:bold>\n                      The Sar1\n                      <jats:styled-content style=\"fixed-case\">GTPase</jats:styled-content>\n                      coordinates the assembly of coat protein complex‐\n                      <jats:styled-content style=\"fixed-case\">II</jats:styled-content>\n                      (\n                      <jats:styled-content style=\"fixed-case\">COPII</jats:styled-content>\n                      ) at specific sites of the endoplasmic reticulum (\n                      <jats:styled-content style=\"fixed-case\">ER</jats:styled-content>\n                      ).\n                      <jats:styled-content style=\"fixed-case\">COPII</jats:styled-content>\n                      is required for\n                      <jats:styled-content style=\"fixed-case\">ER</jats:styled-content>\n                      ‐to‐Golgi transport, as it provides a structural and functional framework to ship out protein cargoes produced in the\n                      <jats:styled-content style=\"fixed-case\">ER</jats:styled-content>\n                      . To investigate the requirement of\n                      <jats:styled-content style=\"fixed-case\">COPII</jats:styled-content>\n                      ‐mediated transport in mammalian cells, we used small interfering\n                      <jats:styled-content style=\"fixed-case\">RNA</jats:styled-content>\n                      (\n                      <jats:styled-content style=\"fixed-case\">siRNA</jats:styled-content>\n                      )‐mediated depletion of\n                      <jats:styled-content style=\"fixed-case\">Sar1A</jats:styled-content>\n                      and\n                      <jats:styled-content style=\"fixed-case\">Sar1B</jats:styled-content>\n                      . We report that depletion of these two mammalian forms of Sar1 disrupts\n                      <jats:styled-content style=\"fixed-case\">COPII</jats:styled-content>\n                      assembly and the cells fail to organize transitional elements that coordinate classical\n                      <jats:styled-content style=\"fixed-case\">ER</jats:styled-content>\n                      ‐to‐Golgi protein transfer. Under these conditions, minimal Golgi stacks are seen in proximity to juxtanuclear\n                      <jats:styled-content style=\"fixed-case\">ER</jats:styled-content>\n                      membranes that contain elements of the intermediate compartment, and from which these stacks coordinate biosynthetic transport of protein cargo, such as the vesicular stomatitis virus G protein and albumin. Here, transport of procollagen‐I is inhibited. These data provide proof‐of‐principle for the contribution of alternative mechanisms that support biosynthetic trafficking in mammalian cells, providing evidence of a functional boundary associated with a bypass of\n                      <jats:styled-content style=\"fixed-case\">COPII</jats:styled-content>\n                    </jats:bold>\n                    .\n                  </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":"23433038","pmcid":null,"openalex_id":"https://openalex.org/W1596180649","authors":[],"funders":[{"funder_name":"Telethon","grant_id":"E.1105","title":null}],"total_grants":1,"fwci":2.9191,"citation_percentile":0.89825299,"influential_citations":5,"citation_trend":[{"year":2013,"count":4},{"year":2014,"count":6},{"year":2015,"count":5},{"year":2016,"count":3},{"year":2017,"count":6},{"year":2018,"count":3},{"year":2019,"count":5},{"year":2020,"count":5},{"year":2021,"count":1},{"year":2022,"count":9},{"year":2023,"count":7},{"year":2024,"count":2},{"year":2025,"count":9},{"year":2026,"count":1}],"oa_status":"closed","license":"http://onlinelibrary.wiley.com/termsAndConditions#vor","oa_locations":[{"url":"https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/tra.12060","host_type":"BRONZE"},{"url":"https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Ftra.12060","host_type":"publisher"},{"url":"https://onlinelibrary.wiley.com/doi/pdf/10.1111/tra.12060","host_type":"publisher"},{"url":"https://doi.org/10.1111/tra.12060","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/23433038","host_type":"repository"}],"fields_of_study":["Cellular transport and secretion","Pancreatic function and diabetes","Endoplasmic Reticulum Stress and Disease","Biology","Medicine","COP-Coated Vesicles","Endoplasmic Reticulum","Gene Silencing","Golgi Apparatus","HeLa Cells","Hep G2 Cells","Humans","Monomeric GTP-Binding Proteins","Procollagen","Protein Isoforms","Protein Transport","RNA, Small Interfering","Secretory Pathway"],"mesh_terms":["Endoplasmic Reticulum","Golgi Apparatus","HeLa Cells","Humans","Procollagen","Protein Isoforms","Monomeric GTP-Binding Proteins","Gene Silencing","Protein Transport","COP-Coated Vesicles","RNA, Small Interfering","Secretory Pathway","Hep G2 Cells","Hela Cells"],"keywords":["COPII","COPI","Cell biology","Golgi apparatus","Endoplasmic reticulum","Biology","Transport protein","Vesicular Transport Proteins","Vesicular transport protein","Secretory pathway","Biochemistry","Endosome","Vesicle","Vacuolar protein sorting","Membrane"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Life below water"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-17T11:37:25.415528Z","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":[]}