Afficher la couverture 'Nuclear magnetic resonance analysis of the acetylation pattern of the neuronal Tau protein. | Kamah, Amina' en grand format
/5

0 avis

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

Archive ouverte

Kamah, Amina | Huvent, Isabelle | Cantrelle, François-Xavier | Qi, Haoling | Lippens, Guy | Landrieu, Isabelle | Smet-Nocca, Caroline

Edité par CCSD ; American Chemical Society -

International audience. 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.

Consulter en ligne

Suggestions

Du même auteur

A functional fragment of Tau forms fibers without the need for an intermolecular cysteine bridge.

Archive ouverte | Huvent, Isabelle | CCSD

International audience. We study the aggregation of a fragment of the neuronal protein Tau that contains part of the proline rich domain and of the microtubule binding repeats. When incubated at 37 °C with heparin, ...

Identification of the Tau phosphorylation pattern that drives its aggregation

Archive ouverte | Despres, Clement | CCSD

International audience. Determining the functional relationship between Tau phosphorylation and aggregation has proven a challenge owing to the multiple potential phosphorylation sites and their clustering in the Ta...

A β-Turn Motif in the Steroid Hormone Receptor’s Ligand-Binding Domains Interacts with the Peptidyl-prolyl Isomerase (PPIase) Catalytic Site of the Immunophilin FKBP52

Archive ouverte | Byrne, Cillian | CCSD

International audience. The immunophilin FKBP52 interacts with nuclear steroid hormone receptors. Studying the crystal structure of human estrogen receptor alpha (hER alpha) and using nuclear magnetic resonance, we ...

Chargement des enrichissements...