Tau aggregation in Alzheimer's disease: what role for phosphorylation?
The crucial role of the neuronal Tau protein in microtubule stabilization and axonal transport suggests that too little or too much Tau might lead to neuronal dysfunction. The presence of a hyper phosphorylated but non aggregated molecule as a toxic species that might sequester normal Tau is discussed. We present recent in vitro results that might allow us to dissect the role of individual phosphorylation sites on its structure and function. We also discuss in this review the role of phosphorylation for the aggregation of the neuronal Tau protein, and compare it to the aggregation induced by external poly anions.
Lippens
Guy
G
CNRS UMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle, Université des Sciences et Technologies de Lille 1, Villeneuve d'Ascq, France. Guy.Lippens@univ-lille1.fr
Sillen
Alain
A
Landrieu
Isabelle
I
Amniai
Laziza
L
Sibille
Nathalie
N
Barbier
Pascale
P
Leroy
Arnaud
A
Hanoulle
Xavier
X
Wieruszeski
Jean-Michel
JM
D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D000818:Animals; D001369:Axons / Q000378:metabolism* / Q000473:pathology; D006801:Humans; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism*; D010766:Phosphorylation; D020836:Protein Structure, Quaternary; D021381:Protein Transport; D013329:Structure-Activity Relationship; D016875:tau Proteins / Q000737:chemistry / Q000378:metabolism*
C054369:MAPT protein, human; D016875:tau Proteins