Acknowledgments
This work was supported by INSERM and Grants from the Association pour la Recherche sur le Cancer (ARC), Agence Nationale de la Recherche (ANR) and Pole de Compétitivité-Medicen (projet Hexocan). C. Clybouw and A. Hadji hold fellowships from Ministère de la Recherche, Fédération de la Recherche Médicale (FRM) and ARC, respectively.
Keywords
Tau; 14-3-3 protein; Phosphorylation; Alzheimer; Frontotemporal dementia
Introduction
Tau is a very soluble protein and does not assemble readily in vitro even at high concentrations. Increasing the levels of tau in both animal and cell culture models through transgenic win 55 212-2 of wild-type human tau at concentrations that saturate the endogenous MT also failed to result in robust tau assembly [9]. However, cofactors, also called exogenous inducers, such as heparin, RNA, glycosaminoglycans, etc. have been found associated with neurofibrillary tangles (NFTs) and promote the aggregation of tau independently of phosphorylation [10], [11] and [12]. Therefore, it seems reasonable to consider that the assembly of tau to form inclusions in vivo also requires the presence of cofactors that might be specific in certain tauopathies and may differentially induce tau aggregation. The identification of such cofactors may provide new insights into the pathogenesis of tauopathy.
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