{"doi":"10.1016/j.celrep.2023.112238","title":"The SOAR of STIM1 interacts with plasma membrane lipids to form ER-PM contact sites","abstract":null,"journal":"Cell Reports","year":2023,"id":632945,"datarank":0.5375278407684165,"base_score":3.58351893845611,"endowment":3.58351893845611,"self_citation_contribution":0.5375278407684165,"citation_network_contribution":0.0,"self_endowment_contribution":0.5375278407684165,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":35,"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":1640840,"name":"Elia Zomot","orcid":null,"position":1,"is_corresponding":false},{"id":1640841,"name":"Tomer Nataniel","orcid":null,"position":2,"is_corresponding":false},{"id":1640842,"name":"Ruslana Militsin","orcid":null,"position":3,"is_corresponding":false},{"id":1640845,"name":"Raz Palty","orcid":"0000-0001-6238-2399","position":4,"is_corresponding":false},{"id":1640839,"name":"Hadas Achildiev Cohen","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"The SOAR of STIM1 interacts with plasma membrane lipids to form ER-PM contact sites","abstract":"Depletion of Ca 2+ from the endoplasmic reticulum (ER) causes the ER Ca 2+ sensor STIM1 to form membrane contact sites (MCSs) with the plasma membrane (PM). At the ER-PM MCS, STIM1 binds to Orai channels to induce cellular Ca 2+ entry. The prevailing view of this sequential process is that STIM1 interacts with the PM and with Orai1 using two separate modules: a C-terminal polybasic domain (PBD) for the interaction with PM phosphoinositides and the STIM-Orai activation region (SOAR) for the interaction with Orai channels. Here, using electron and fluorescence microscopy and protein-lipid interaction assays, we show that oligomerization of the SOAR promotes direct interaction with PM phosphoinositides to trap STIM1 at ER-PM MCSs. The interaction depends on a cluster of conserved lysine residues within the SOAR and is co-regulated by the STIM1 coil-coiled 1 and inactivation domains. Collectively, our findings uncover a molecular mechanism for formation and regulation of ER-PM MCSs by STIM1.","is_dataset_classified":null,"base_score":3.58351893845611,"endowment":3.58351893845611,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"36906853","pmcid":null,"openalex_id":"https://openalex.org/W4323830122","authors":[],"funders":[{"funder_name":"Israel Science Foundation","grant_id":"1048/18","title":null},{"funder_name":"Israel Science Foundation","grant_id":"2123/22","title":null}],"total_grants":2,"fwci":5.6557,"citation_percentile":0.97413156,"influential_citations":0,"citation_trend":[{"year":2023,"count":3},{"year":2024,"count":13},{"year":2025,"count":9},{"year":2026,"count":10}],"oa_status":"gold","license":"cc-by-nc-nd","oa_locations":[{"url":"https://doi.org/10.1016/j.celrep.2023.112238","host_type":"journal"},{"url":"https://doi.org/10.1016/j.celrep.2023.112238","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S2211124723002498?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S2211124723002498?httpAccept=text/plain","host_type":"publisher"},{"url":"https://pubmed.ncbi.nlm.nih.gov/36906853","host_type":"repository"},{"url":"https://doaj.org/article/a264906937de4dc982e3e3d6008193f1","host_type":"repository"}],"fields_of_study":["Ion Channels and Receptors","Neurobiology and Insect Physiology Research","Phytochemicals and Antioxidant Activities","ORAI1 Protein","Cell Membrane","Endoplasmic Reticulum","Phosphatidylinositols","Stromal Interaction Molecule 1","Calcium","Calcium Signaling"],"mesh_terms":["Stromal Interaction Molecule 1","ORAI1 Protein","Calcium","Cell Membrane","Endoplasmic Reticulum","Phosphatidylinositols","Calcium Signaling"],"keywords":["STIM1","Endoplasmic reticulum","Chemistry","Cell biology","ORAI1","Bimolecular fluorescence complementation","Biophysics","Membrane","Biochemistry","Biology","Yeast","Calcium","Polyphosphoinositides","Crac Channel","Soce","Soar","Stim2","Membrane Contact Sites (Mcss)","Er-pm Contact Sites","Cp: Cell Biology"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-06T10:37:53.086527Z","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":[]}