{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Boopathy S"],"pubmed_abstract":["Mitochondrial fusion requires the sequential merger of four bilayers to two. The outer-membrane solute carrier protein SLC25A46 interacts with both the outer and inner-membrane dynamin family GTPases Mfn1/2 and Opa1. While SLC25A46 levels are known affect mitochondrial morphology, how SLC25A46 interacts with Mfn1/2 and Opa1 to regulate membrane fusion is not understood. In this study, we use crosslinking mass-spectrometry and AlphaFold 2 modeling to identify interfaces mediating a SLC25A46-Opa1-Mfn1/2 complex. We reveal that the bundle signaling element of Opa1 interacts with SLC25A46, and the helical repeat 1 region of Mfn2 interacts with the SLC25A46 N-terminus. We validate these newly identified interaction interfaces and show that they play a role in mitochondrial network maintenance."],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2023.12.29.573615"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10793391"],"repository":["biostudies-literature"],"pubmed_title":["Identification of SLC25A46 interaction interfaces with mitochondrial membrane fusogens Mfn2 and Opa1."],"pmcid":["PMC10793391"],"pubmed_authors":["Ponce J","Boopathy S","McDonald J","Luce BE","Chao LH","Makhlouta Lugo C","Hakim P","Ueberheide BM"],"additional_accession":[]},"is_claimable":false,"name":"Identification of SLC25A46 interaction interfaces with mitochondrial membrane fusogens Mfn2 and Opa1.","description":"Mitochondrial fusion requires the sequential merger of four bilayers to two. The outer-membrane solute carrier protein SLC25A46 interacts with both the outer and inner-membrane dynamin family GTPases Mfn1/2 and Opa1. While SLC25A46 levels are known affect mitochondrial morphology, how SLC25A46 interacts with Mfn1/2 and Opa1 to regulate membrane fusion is not understood. In this study, we use crosslinking mass-spectrometry and AlphaFold 2 modeling to identify interfaces mediating a SLC25A46-Opa1-Mfn1/2 complex. We reveal that the bundle signaling element of Opa1 interacts with SLC25A46, and the helical repeat 1 region of Mfn2 interacts with the SLC25A46 N-terminus. We validate these newly identified interaction interfaces and show that they play a role in mitochondrial network maintenance.","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Dec","modification":"2025-04-25T23:24:43.599Z","creation":"2025-04-06T09:24:24.818Z"},"accession":"S-EPMC10793391","cross_references":{"pubmed":["38234813"],"doi":["10.1101/2023.12.29.573615"]}}