NMR analysis of the acetylation pattern of the neuronal Tau protein.
NMR analysis of the acetylation pattern of the neuronal Tau protein.
Biochemistry. 2014 Apr 7;
Authors: Kamah A, Huvent I, Cantrelle FX, Qi H, Lippens G, Landrieu I, Smet-Nocca C
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 NMR spectroscopy. Our study gives a quantitative overview of CBP-mediated acetylation and examines the catalytic proficiency since non-enzymatic 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.
PMID: 24708343 [PubMed - as supplied by publisher]
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