Our work is focused in the characterization of physiological roles of the death receptor antagonist, FAIM-L. We had previously evidenced its interaction in neurons with XIAP and Siva-1, confirming that FAIM-L is involved in neuronal plasticity processes by modulating caspases activity. We have characterized an interaction in vitro and in vivo of FAIM-L with tau, a key protein in Alzheimer’s disease (AD), and how FAIM-L is post-translationally modifying tau protein, thus showing the relevance of FAIM-L in the development of tauopathies and neurodegenerative processes. In addition, our results show a key role for FAIM-L in retinal homeostasis, by controlling glial response, ubiquitinated protein aggregation, vascular leakage, and photoreceptor signaling and survival. We are also developing new tools to better characterize FAIM-L expression and to modulate its levels in different animal models of AD, with the aim to better knowing its role in neuron physiology and neurodegeneration.
eCOREs
