{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tavoulari S"],"funding":["Citrin Foundation","Swiss National Science Foundation","Medical Research Council","UK Research and Innovation Medical Research Council"],"pagination":["102047"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11539162"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["90"],"pubmed_abstract":["Objective
Citrin, the mitochondrial aspartate/glutamate carrier isoform 2 (AGC2), is structurally and mechanistically the most complex SLC25 family member, because it consists of three domains and forms a homo-dimer. Each protomer has an N-terminal calcium-binding domain with EF-hands, followed by a substrate-transporting carrier domain and a C-terminal domain with an amphipathic helix. The absence or dysfunction of citrin leads to citrin deficiency, a highly prevalent pan-ethnic mitochondrial disease. Here, we aim to understand the role of different citrin domains and how they contribute to pathogenic mechanisms in citrin deficiency.Methods
We have employed structural modeling and functional reconstitution of purified proteins in proteoliposomes to assess the transport act"],"journal":["Molecular metabolism"],"pubmed_title":["Distinct roles for the domains of the mitochondrial aspartate/glutamate carrier citrin in organellar localization and substrate transport."],"pmcid":["PMC11539162"],"funding_grant_id":["MC_UU_00028/2","MC_UU_00028/5","180326","MC_UU_00015/7"],"pubmed_authors":["Tavoulari S","Pereira GC","King MS","Palmer SM","He J","Chowdhury SR","Kunji ERS","Thangaratnarajah C","Lacabanne D","Tilokani L","Walker JE","Prudent J"],"additional_accession":[]},"is_claimable":false,"name":"Distinct roles for the domains of the mitochondrial aspartate/glutamate carrier citrin in organellar localization and substrate transport.","description":"Objective
Citrin, the mitochondrial aspartate/glutamate carrier isoform 2 (AGC2), is structurally and mechanistically the most complex SLC25 family member, because it consists of three domains and forms a homo-dimer. Each protomer has an N-terminal calcium-binding domain with EF-hands, followed by a substrate-transporting carrier domain and a C-terminal domain with an amphipathic helix. The absence or dysfunction of citrin leads to citrin deficiency, a highly prevalent pan-ethnic mitochondrial disease. Here, we aim to understand the role of different citrin domains and how they contribute to pathogenic mechanisms in citrin deficiency.Methods
We have employed structural modeling and functional reconstitution of purified proteins in proteoliposomes to assess the transport act","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-06-01T15:22:11.858Z","creation":"2025-04-04T01:45:13.974Z"},"accession":"S-EPMC11539162","cross_references":{"pubmed":["39419476"],"doi":["10.1016/j.molmet.2024.102047"]}}