{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["285(43)"],"submitter":["Leroy A"],"pubmed_abstract":["Alzheimer disease neurons are characterized by extraneuronal plaques formed by aggregated amyloid-β peptide and by intraneuronal tangles composed of fibrillar aggregates of the microtubule-associated Tau protein. Tau is mostly found in a hyperphosphorylated form in these tangles. Glycogen synthase kinase 3β (GSK3β) is a proline-directed kinase generally considered as one of the major players that (hyper)phosphorylates Tau. The kinase phosphorylates mainly (Ser/Thr)-Pro motifs and is believed to require a priming activity by another kinase. Here, we use an in vitro phosphorylation assay and NMR spectroscopy to characterize in a qualitative and quantitative manner the phosphorylation of Tau by GSK3β. We find that three residues can be phosphorylated (Ser-396, Ser-400, and Ser-404) by GSK3β a"],"journal":["The Journal of biological chemistry"],"pagination":["33435-33444"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2963357"],"repository":["biostudies-literature"],"pubmed_title":["Spectroscopic studies of GSK3{beta} phosphorylation of the neuronal tau protein and its interaction with the N-terminal domain of apolipoprotein E."],"pmcid":["PMC2963357"],"pubmed_authors":["Landrieu I","Codeville B","Wieruszeski JM","Huvent I","Leroy A","Legrand D","Lippens G"],"additional_accession":[]},"is_claimable":false,"name":"Spectroscopic studies of GSK3{beta} phosphorylation of the neuronal tau protein and its interaction with the N-terminal domain of apolipoprotein E.","description":"Alzheimer disease neurons are characterized by extraneuronal plaques formed by aggregated amyloid-β peptide and by intraneuronal tangles composed of fibrillar aggregates of the microtubule-associated Tau protein. Tau is mostly found in a hyperphosphorylated form in these tangles. Glycogen synthase kinase 3β (GSK3β) is a proline-directed kinase generally considered as one of the major players that (hyper)phosphorylates Tau. The kinase phosphorylates mainly (Ser/Thr)-Pro motifs and is believed to require a priming activity by another kinase. Here, we use an in vitro phosphorylation assay and NMR spectroscopy to characterize in a qualitative and quantitative manner the phosphorylation of Tau by GSK3β. We find that three residues can be phosphorylated (Ser-396, Ser-400, and Ser-404) by GSK3β a","dates":{"release":"2010-01-01T00:00:00Z","publication":"2010 Oct","modification":"2025-04-26T11:27:03.046Z","creation":"2019-03-27T00:35:05Z"},"accession":"S-EPMC2963357","cross_references":{"pubmed":["20679343"],"doi":["10.1074/jbc.M110.149419","10.1074/jbc.m110.149419"]}}