NMR Meets Tau: Insights into Its Function and Pathology

Guy Lippens (1, 2) , Isabelle Landrieu (2) , Caroline Smet (2) , Isabelle Huvent (2) , Neha Gandhi (3) , Benoît Gigant (4) , Clément Despres (2) , Haoling Qi (2) , Juan Lopez (2)

1 LISBP - Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés
2 UGSF - Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576
3 School of Mathematical Sciences, Queensland University of Technology
4 I2BC - Institut de Biologie Intégrative de la Cellule

In this review, we focus on what we have learned from Nuclear Magnetic Resonance (NMR) studies on the neuronal microtubule-associated protein Tau. We consider both the mechanistic details of Tau: the tubulin relationship and its aggregation process. Phosphorylation of Tau is intimately linked to both aspects. NMR spectroscopy has depicted accurate phosphorylation patterns by different kinases, and its non-destructive character has allowed functional assays with the same samples. Finally, we will discuss other post-translational modifications of Tau and its interaction with other cellular factors in relationship to its (dys)function.

Mots clés: NMR spectroscopy; intrinsically disordered protein; aggregation; phosphorylation

Mots clés: Tau; tubulin; protein; protein interactions

Domaines: Biochimie [q-bio.BM]

Guy Lippens, Isabelle Landrieu, Caroline Smet, Isabelle Huvent, Neha Gandhi, et al.. NMR Meets Tau: Insights into Its Function and Pathology. Ancient biomolecules, 2016, 6 (2), ⟨10.3390/biom6020028⟩. ⟨hal-01389829⟩