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.
NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease
Isabelle Landrieu, Arnaud Leroy, Caroline Smet-Nocca, Isabelle Huvent, Laziza Amniai, Malika Hamdane, Nathalie Sibille, Luc Buée, Jean-Michel Wieruszeski, Guy Lippens; NMR spectroscopy of the neuronal tau protein: normal function and implication in Alzheimer's disease. Biochem Soc Trans 1 August 2010; 38 (4): 1006–1011. doi: https://doi.org/10.1042/BST0381006
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