NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease. - CNRS - Centre national de la recherche scientifique Accéder directement au contenu
Article Dans Une Revue Biochemical Society Transactions Année : 2010

NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease.

Résumé

NMR spectroscopy was used to explore the different aspects of the normal and pathological functions of tau, but proved challenging because the protein contains 441 amino acids and has poor signal dispersion. We have set out to dissect the phosphorylation patterns of tau in order to understand better its role in the aggregation process and microtubule-binding regulation. Our current knowledge on the functional consequences of specific phosphorylations is still limited, mainly because producing and assessing quantitatively phosphorylated tau samples is far from straightforward, even in vitro. We use NMR spectroscopy as a proteomics tool to characterize the phosphorylation patterns of tau, after in vitro phosphorylation by recombinant kinases. The phosphorylated tau can next be use for functional assays or interaction assays with phospho-dependent protein partners, such as the prolyl cis-trans isomerase Pin1.
Fichier non déposé

Dates et versions

hal-00586933 , version 1 (18-04-2011)

Identifiants

Citer

Isabelle Landrieu, Arnaud Leroy, Caroline Smet-Nocca, Isabelle Huvent, Laziza Amniai, et al.. NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease.. Biochemical Society Transactions, 2010, 38 (4), pp.1006-11. ⟨10.1042/BST0381006⟩. ⟨hal-00586933⟩

Collections

CNRS UNIV-LILLE
46 Consultations
0 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More