{"doi":"10.1242/jcs.132001","title":"Osh proteins regulate COPII-mediated vesicular transport of ceramide from the endoplasmic reticulum in budding yeast","abstract":"<jats:p>Lipids synthesized at the endoplasmic reticulum (ER) are delivered to the Golgi by vesicular and non-vesicular pathways. ER-to-Golgi transport is critical for maintaining the different membrane lipid composition and identities of organelles. Despite their importance, mechanisms regulating transport remain elusive. Here we report that coat protein complex II (COPII) vesicle-mediated transport of ceramide from the ER to the Golgi requires the yeast oxysterol-binding protein homologs, Osh proteins, which have been implicated in lipid homeostasis. Because Osh proteins are not required to transport proteins to the Golgi, these results indicate a specific requirement for the Osh proteins in the transport of ceramide. In addition, we provide evidence that Osh proteins play a negative role in COPII vesicle biogenesis. Together, our data suggest that ceramide transport and sphingolipid levels between the ER and Golgi are maintained by two distinct functions of Osh proteins, which negatively regulate COPII vesicle formation and positively control the late stage, presumably fusion of ceramide-enriched vesicles with Golgi compartments.</jats:p>","journal":"Journal of Cell Science","year":2013,"id":47152,"datarank":1.4964518629033932,"base_score":3.784189633918261,"endowment":3.784189633918261,"self_citation_contribution":0.5676284450877392,"citation_network_contribution":0.9288234178156538,"self_endowment_contribution":0.5676284450877392,"citer_contribution":0.9288234178156538,"corpus_percentile":null,"corpus_rank":null,"citation_count":43,"citer_count":29,"citers_with_citation_signal":24,"citers_with_endowment":24,"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":217668,"name":"Atsuko Ikeda","orcid":null,"position":1,"is_corresponding":false},{"id":123372,"name":"Auxiliadora Aguilera-Romero","orcid":null,"position":2,"is_corresponding":false},{"id":173586,"name":"Guillaume A. 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ER-to-Golgi transport is critical for maintaining the different membrane lipid composition and identities of organelles. Despite their importance, mechanisms regulating transport remain elusive. Here we report that coat protein complex II (COPII) vesicle-mediated transport of ceramide from the ER to the Golgi requires the yeast oxysterol-binding protein homologs, Osh proteins, which have been implicated in lipid homeostasis. Because Osh proteins are not required to transport proteins to the Golgi, these results indicate a specific requirement for the Osh proteins in the transport of ceramide. In addition, we provide evidence that Osh proteins play a negative role in COPII vesicle biogenesis. Together, our data suggest that ceramide transport and sphingolipid levels between the ER and Golgi are maintained by two distinct functions of Osh proteins, which negatively regulate COPII vesicle formation and positively control the late stage, presumably fusion of ceramide-enriched vesicles with Golgi compartments.</jats:p>","is_dataset_classified":null,"base_score":3.784189633918261,"endowment":3.784189633918261,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"24213531","pmcid":null,"openalex_id":"https://openalex.org/W2061137874","authors":[],"funders":[{"funder_name":"Swiss National Science Foundation","grant_id":"146142","title":"Lipid homeostasis and function"}],"total_grants":1,"fwci":2.4326,"citation_percentile":0.87483824,"influential_citations":2,"citation_trend":[{"year":2014,"count":1},{"year":2015,"count":6},{"year":2016,"count":8},{"year":2017,"count":1},{"year":2018,"count":6},{"year":2019,"count":3},{"year":2020,"count":4},{"year":2021,"count":2},{"year":2022,"count":2},{"year":2023,"count":6},{"year":2024,"count":2},{"year":2026,"count":2}],"oa_status":"bronze","license":"CC BY NC ND","oa_locations":[{"url":"https://jcs.biologists.org/content/joces/127/2/376.full.pdf","host_type":"journal"},{"url":"https://jcs.biologists.org/content/joces/127/2/376.full.pdf","host_type":"BRONZE"},{"url":"https://jcs.biologists.org/content/joces/127/2/376.full.pdf","host_type":"publisher"},{"url":"http://journals.biologists.com/jcs/article-pdf/127/2/376/1960772/jcs-127-02-0376.pdf","host_type":"publisher"},{"url":"http://journals.biologists.com/jcs/article-pdf/doi/10.1242/jcs.132001/2045756/jcs132001.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1242/jcs.132001","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/24213531","host_type":"repository"},{"url":"https://idus.us.es/handle/11441/64850","host_type":"repository"},{"url":"http://jcs.biologists.org/cgi/content/short/127/2/376","host_type":"repository"},{"url":"https://idus.us.es/bitstream/11441/64850/1/Osh%20proteins%20regulate.pdf","host_type":""},{"url":"http://hdl.handle.net/11441/64850","host_type":""},{"url":"https://dx.doi.org/10.1242/jcs.132001","host_type":""},{"url":"http://dx.doi.org/10.1242/jcs.132001","host_type":""}],"fields_of_study":["Cellular transport and secretion","Lipid Membrane Structure and Behavior","Sphingolipid Metabolism and Signaling","Medicine","Biology","Chemistry","0301 basic medicine","0303 health sciences","03 medical and health sciences","Biological Transport","COP-Coated Vesicles","Cell Compartmentation","Ceramides","Endoplasmic Reticulum","Gene Deletion","Golgi Apparatus","Humans","Models, Biological","Saccharomyces cerevisiae Proteins","Saccharomycetales","Transport Vesicles"],"mesh_terms":["Biological Transport","Cell Compartmentation","Ceramides","Saccharomycetales","Endoplasmic Reticulum","Golgi Apparatus","Humans","Models, Biological","Gene Deletion","Transport Vesicles","COP-Coated Vesicles","Saccharomyces cerevisiae Proteins"],"keywords":["COPII","COPI","Golgi apparatus","Endoplasmic reticulum","Cell biology","Biology","Ceramide","Vesicular transport protein","Vesicular Transport Proteins","Vesicle","Transport protein","Secretory pathway","Sphingomyelin","Sphingolipid","Biochemistry","Cytoplasm","Vacuole","Membrane","Yeast","Vesicular Transport","Oxysterol-binding Protein","Saccharomyces cerevisiae Proteins","Biological Transport","Ceramides","Models, Biological","Cell Compartmentation","Saccharomycetales","Humans","COP-Coated Vesicles","Transport Vesicles","Gene Deletion"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-07-17T10:09:08.162717Z","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":[]}