{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["299(6)"],"submitter":["Ruiz M"],"pubmed_abstract":["The human AdipoR2 and its Caenorhabditis elegans homolog PAQR-2 are multipass plasma membrane proteins that protect cells against membrane rigidification. However, how AdipoR2 promotes membrane fluidity mechanistically is not clear. Using 13C-labeled fatty acids, we show that AdipoR2 can promote the elongation and incorporation of membrane-fluidizing polyunsaturated fatty acids into phospholipids. To elucidate the molecular basis of these activities, we performed immunoprecipitations of tagged AdipoR2 and PAQR-2 expressed in HEK293 cells or whole C. elegans, respectively, and identified coimmunoprecipitated proteins using mass spectrometry. We found that several of the evolutionarily conserved AdipoR2/PAQR-2 interactors are important for fatty acid elongation and incorporation into phospho"],"journal":["The Journal of biological chemistry"],"pagination":["104799"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10279913"],"repository":["biostudies-literature"],"pubmed_title":["AdipoR2 recruits protein interactors to promote fatty acid elongation and membrane fluidity."],"pmcid":["PMC10279913"],"pubmed_authors":["Ruhanen H","Boren J","Devkota R","Henricsson M","Kaper D","Busayavalasa K","Pilon M","Kakela R","Radovic U","Ruiz M"],"additional_accession":[]},"is_claimable":false,"name":"AdipoR2 recruits protein interactors to promote fatty acid elongation and membrane fluidity.","description":"The human AdipoR2 and its Caenorhabditis elegans homolog PAQR-2 are multipass plasma membrane proteins that protect cells against membrane rigidification. However, how AdipoR2 promotes membrane fluidity mechanistically is not clear. Using 13C-labeled fatty acids, we show that AdipoR2 can promote the elongation and incorporation of membrane-fluidizing polyunsaturated fatty acids into phospholipids. To elucidate the molecular basis of these activities, we performed immunoprecipitations of tagged AdipoR2 and PAQR-2 expressed in HEK293 cells or whole C. elegans, respectively, and identified coimmunoprecipitated proteins using mass spectrometry. We found that several of the evolutionarily conserved AdipoR2/PAQR-2 interactors are important for fatty acid elongation and incorporation into phospho","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jun","modification":"2026-04-12T23:13:30.503Z","creation":"2025-04-04T11:50:09.161Z"},"accession":"S-EPMC10279913","cross_references":{"pubmed":["37164154"],"doi":["10.1016/j.jbc.2023.104799"]}}