{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Isei MO"],"funding":["NIA NIH HHS"],"pubmed_abstract":["Phosphorylation of tau at sites associated with Alzheimer's disease (AD) likely plays a role in the disease progression. Mitochondrial impairment, correlating with increased presence of phosphorylated tau, has been identified as a contributing factor to neurodegenerative processes in AD. However, how tau phosphorylated at specific sites impacts mitochondrial function has not been fully defined. We examined how AD-relevant phosphomimetics of tau impact selected aspects of mitochondrial biology. To mimic phosphorylation at AD-associated sites, the Ser/Thr sites in wild-type GFP tagged-tau (T4) were converted to glutamic acid (E) to make pseudophosphorylated GFP tagged-Ser-396/404 (2EC) and GFP tagged-Thr-231/Ser-235 (2EM) constructs. These constructs were expressed in neuronal HT22 cells and"],"journal":["bioRxiv : the preprint server for biology"],"pagination":["2023.02.19.529131"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9949115"],"repository":["biostudies-literature"],"pubmed_title":["Site-specific phosphorylation of tau impacts mitochondrial biology and response to stressors."],"pmcid":["PMC9949115"],"funding_grant_id":["R01 AG067617"],"pubmed_authors":["Johnson GV","Rodwell-Bullock J","Isei MO","Girardi PA","Nehrke K"],"additional_accession":[]},"is_claimable":false,"name":"Site-specific phosphorylation of tau impacts mitochondrial biology and response to stressors.","description":"Phosphorylation of tau at sites associated with Alzheimer's disease (AD) likely plays a role in the disease progression. Mitochondrial impairment, correlating with increased presence of phosphorylated tau, has been identified as a contributing factor to neurodegenerative processes in AD. However, how tau phosphorylated at specific sites impacts mitochondrial function has not been fully defined. We examined how AD-relevant phosphomimetics of tau impact selected aspects of mitochondrial biology. To mimic phosphorylation at AD-associated sites, the Ser/Thr sites in wild-type GFP tagged-tau (T4) were converted to glutamic acid (E) to make pseudophosphorylated GFP tagged-Ser-396/404 (2EC) and GFP tagged-Thr-231/Ser-235 (2EM) constructs. These constructs were expressed in neuronal HT22 cells and","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Feb","modification":"2025-04-18T12:50:11.094Z","creation":"2025-02-19T04:54:55.188Z"},"accession":"S-EPMC9949115","cross_references":{"pubmed":["36824940"],"doi":["10.1101/2023.02.19.529131"]}}