{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Karakas E"],"funding":["HHS | NIH | National Institute of Diabetes and Digestive and Kidney Diseases (NIDDK)","NIDDK NIH HHS","National Institute of Diabetes and Digestive and Kidney Diseases","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["4201-4211"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12333906"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["603(15)"],"pubmed_abstract":["Volume-regulated anion channels (VRACs) encoded by the LRRC8 gene family play essential roles in diverse and fundamentally important physiological processes in vertebrate cells. The recent determination of high-resolution cryo-electron microscopy (cryo-EM) structures of homomeric and heteromeric LRRC8 channel complexes has created unprecedented opportunities for understanding the molecular basis of VRAC structure, function and pharmacology. Native LRRC8 channels are obligatory heteromers composed of at least one LRRC8A subunit together with one of the other paralogues (LRRC8B-E) with an unknown stoichiometry. This heteromeric nature of endogenously expressed VRACs and the difficulties associated with controlling the composition and stoichiometry of heterologously expressed LRRC8 channels p"],"journal":["The Journal of physiology"],"pubmed_title":["Recent advances in structural characterization of volume-regulated anion channels (VRACs)."],"pmcid":["PMC12333906"],"funding_grant_id":["R01GM141251","R01DK051610","R01 DK051610"],"pubmed_authors":["Karakas E","Denton JS","Strange K"],"additional_accession":[]},"is_claimable":false,"name":"Recent advances in structural characterization of volume-regulated anion channels (VRACs).","description":"Volume-regulated anion channels (VRACs) encoded by the LRRC8 gene family play essential roles in diverse and fundamentally important physiological processes in vertebrate cells. The recent determination of high-resolution cryo-electron microscopy (cryo-EM) structures of homomeric and heteromeric LRRC8 channel complexes has created unprecedented opportunities for understanding the molecular basis of VRAC structure, function and pharmacology. Native LRRC8 channels are obligatory heteromers composed of at least one LRRC8A subunit together with one of the other paralogues (LRRC8B-E) with an unknown stoichiometry. This heteromeric nature of endogenously expressed VRACs and the difficulties associated with controlling the composition and stoichiometry of heterologously expressed LRRC8 channels p","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Aug","modification":"2026-04-15T19:19:15.194Z","creation":"2026-04-07T14:01:27.093Z"},"accession":"S-EPMC12333906","cross_references":{"pubmed":["39977537"],"doi":["10.1113/JP286189"]}}