Proline Conformation in a Functional Tau Fragment

Puneet Ahuja, François Xavier Cantrelle, Isabelle Huvent, Xavier Hanoulle, Juan Lopez, Caroline Smet, Jean Michel Wieruszeski, Isabelle Landrieu, G. Lippens

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

31 Citas (Scopus)


The conformational state of distinct prolines can determine the folding of a protein but equally other biological processes when coupled to a conformation-sensitive secondary reaction. For the neuronal tau protein, the importance of proline conformation is underscored by its interaction with different prolyl cis/trans isomerases. The proline conformation would gain even further importance after phosphorylation of the preceding residue by various proline-directed kinases. A number of molecular diseases including Alzheimer's disease and traumatic brain injury were thereby recently qualified as "cistauosis", as they would imply a cis conformation for the pThr231-Pro232 prolyl bond. We here investigate by NMR spectroscopy the conformation of all prolines in a functional Tau fragment, Tau[208-324]. Although we can detect and identify some minor conformers in the cis form, we show that all prolines are for over 90% in the trans conformation. Phosphorylation by CDK2/CycA3, which notably leads to complete modification of the Thr231 residue, does not change this conclusion. Our data hence disagree with the notion that specific prolyl bonds in tau would adopt preferentially the cis conformation.

Idioma originalInglés
Páginas (desde-hasta)79-91
Número de páginas13
PublicaciónJournal of Molecular Biology
EstadoPublicada - 16 ene. 2016
Publicado de forma externa


Profundice en los temas de investigación de 'Proline Conformation in a Functional Tau Fragment'. En conjunto forman una huella única.

Citar esto