{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Yablonska S"],"funding":["NIA NIH HHS","National Institute for Health Research (NIHR)","NINDS NIH HHS","NCI NIH HHS"],"pagination":["16593-16602"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6697818"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["116(33)"],"pubmed_abstract":["Mutant huntingtin (mHTT), the causative protein in Huntington's disease (HD), associates with the translocase of mitochondrial inner membrane 23 (TIM23) complex, resulting in inhibition of synaptic mitochondrial protein import first detected in presymptomatic HD mice. The early timing of this event suggests that it is a relevant and direct pathophysiologic consequence of mHTT expression. We show that, of the 4 TIM23 complex proteins, mHTT specifically binds to the TIM23 subunit and that full-length wild-type huntingtin (wtHTT) and mHTT reside in the mitochondrial intermembrane space. We investigated differences in mitochondrial proteome between wtHTT and mHTT cells and found numerous proteomic disparities between mHTT and wtHTT mitochondria. We validated these data by quantitative immunobl"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Mutant huntingtin disrupts mitochondrial proteostasis by interacting with TIM23."],"pmcid":["PMC6697818"],"funding_grant_id":["P50 AG008702","P30 CA047904","R01NS039324","R01 NS039324"],"pubmed_authors":["Chen N","Stevens DA","Chang YF","Schurdak ME","Pyzel A","Minden JS","Kim J","Friedlander RM","Ferrando LM","Ganesan V","Strohlein CE","Baranova OV","Khattar NK","Baranov SV","Wang X","Larkin TM","Yablonska S","Carlisle DL"],"additional_accession":[]},"is_claimable":false,"name":"Mutant huntingtin disrupts mitochondrial proteostasis by interacting with TIM23.","description":"Mutant huntingtin (mHTT), the causative protein in Huntington's disease (HD), associates with the translocase of mitochondrial inner membrane 23 (TIM23) complex, resulting in inhibition of synaptic mitochondrial protein import first detected in presymptomatic HD mice. The early timing of this event suggests that it is a relevant and direct pathophysiologic consequence of mHTT expression. We show that, of the 4 TIM23 complex proteins, mHTT specifically binds to the TIM23 subunit and that full-length wild-type huntingtin (wtHTT) and mHTT reside in the mitochondrial intermembrane space. We investigated differences in mitochondrial proteome between wtHTT and mHTT cells and found numerous proteomic disparities between mHTT and wtHTT mitochondria. We validated these data by quantitative immunobl","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Aug","modification":"2025-04-19T19:46:09.616Z","creation":"2025-04-19T19:46:09.616Z"},"accession":"S-EPMC6697818","cross_references":{"pubmed":["31346086"],"doi":["10.1073/pnas.1904101116"]}}