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Nuclear magnetic resonance analysis of the acetylation pattern of the neuronal Tau protein.

Abstract : Lysine acetylation of the neuronal Tau protein was described as a novel mechanism of posttranslational regulation of Tau functions with important outcomes in microtubule binding and aggregation processes related to Alzheimer's disease. Here, we unravel at a per-residue resolution the acetylation pattern of full-length Tau by the Creb-binding protein (CBP) acetyltransferase using high-resolution nuclear magnetic resonance spectroscopy. Our study gives a quantitative overview of CBP-mediated acetylation and examines the catalytic proficiency because the nonenzymatic reaction with acetyl-coenzyme A occurs in vitro. Furthermore, we have investigated with this characterized acetylated Tau the effect of acetylation on Tau fibrillization in a heparin-induced aggregation assay and on heparin binding.
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https://hal.archives-ouvertes.fr/hal-01077868
Contributor : Isabelle Landrieu <>
Submitted on : Monday, October 27, 2014 - 2:12:23 PM
Last modification on : Friday, August 7, 2020 - 11:40:13 AM

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Amina Kamah, Isabelle Huvent, François-Xavier Cantrelle, Haoling Qi, Guy Lippens, et al.. Nuclear magnetic resonance analysis of the acetylation pattern of the neuronal Tau protein.. Biochemistry, American Chemical Society, 2014, 53 (18), pp.3020-32. ⟨10.1021/bi500006v⟩. ⟨hal-01077868⟩

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