{"doi":"10.1016/j.bbamem.2025.184454","title":"Small angle neutron scattering study of rhodopsin oligomerization and G-protein coupling in a physiologically relevant lipid membrane","abstract":"Although the oligomeric states of G-protein-coupled receptors (GPCRs) and interactions with cognate G proteins are central to their signal transduction capabilities, they remain poorly defined. In this study, we used small-angle neutron scattering (SANS) and a neutron contrast matching approach to elucidate the oligomeric states of the archetypal GPCR, rhodopsin, and its interaction with the G protein transducin (G t ). At a rhodopsin/lipid molar ratio of 1/360, we found that dark-adapted rhodopsin exists as a monomer, a finding consistent with its high functional activity measured upon photoactivation by spectrophotometry and the rate of catalyzed [ 35 S]-GTP-γ-S exchange. Following light activation, we observed that rhodopsin forms a stable 1:1 stoichiometric complex with G t , the structure of which is consistent with recent cryo-EM data. In contrast, activated rhodopsin in the absence of G t showed a propensity to form higher order oligomers. This research underscores the concentration-dependent nature of rhodopsin oligomerization and establishes SANS and the ability to produce appropriately contrast-matched samples, as a robust strategy for characterizing integral membrane protein interactions under biologically relevant conditions.","journal":"Biochimica et Biophysica Acta (BBA) - Biomembranes","year":2025,"id":534707,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":2,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":0.9499,"is_data_producer":false,"deposit_databanks":null,"is_oa":true,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":"2025-01-01","fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1417840,"name":"Jonathan D. Nickels","orcid":"0000-0001-8351-7846","position":1,"is_corresponding":false},{"id":379908,"name":"Kirk G. Hines","orcid":null,"position":2,"is_corresponding":false},{"id":785187,"name":"Walter E. Teague","orcid":null,"position":3,"is_corresponding":false},{"id":1418365,"name":"John K. Northup","orcid":null,"position":4,"is_corresponding":false},{"id":229051,"name":"John Katsaras","orcid":"0000-0002-8937-4177","position":5,"is_corresponding":false},{"id":378872,"name":"Klaus Gawrisch","orcid":"0000-0002-0841-1539","position":6,"is_corresponding":false},{"id":356213,"name":"Olivier Soubias","orcid":"0000-0003-4819-2753","position":0,"is_corresponding":true}],"reference_count":40,"raw_metadata":null,"created_at":"2026-07-19T02:51:52.019261Z","pmid":"40945563","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":[]}