Nuclear magnetic resonance analysis of the acetylation pattern of the neuronal Tau protein. - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Biochemistry Année : 2014

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

Résumé

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.
Fichier non déposé

Dates et versions

hal-01077868 , version 1 (27-10-2014)

Identifiants

Citer

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, 2014, 53 (18), pp.3020-32. ⟨10.1021/bi500006v⟩. ⟨hal-01077868⟩

Collections

CNRS UNIV-LILLE
49 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More