Lippens Guy, Sillen Alain, Landrieu Isabelle, Amniai Laziza, Sibille Nathalie, Barbier Pascale, Leroy Arnaud, Hanoulle Xavier, Wieruszeski Jean-Michel
CNRS UMR 8576, Unité de Glycobiologie Structurale et Fonctionnelle, Université des Sciences et Technologies de Lille 1, Villeneuve d'Ascq, France.
Prion. 2007 Jan-Mar;1(1):21-5. doi: 10.4161/pri.1.1.4055. Epub 2007 Jan 23.
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.
神经元 Tau 蛋白在微管稳定和轴突运输中的关键作用表明,Tau 蛋白过少或过多都可能导致神经元功能障碍。本文讨论了一种过度磷酸化但未聚集的分子作为可能隔离正常 Tau 的毒性物质的存在。我们展示了最近的体外实验结果,这些结果可能使我们能够剖析单个磷酸化位点在其结构和功能上的作用。在这篇综述中,我们还讨论了磷酸化在神经元 Tau 蛋白聚集中的作用,并将其与外部多阴离子诱导的聚集进行比较。