Our work is focused in the characterization of the physiological roles of the death receptor antagonist, FAIM-L. We have evidenced its interaction in neurons with XIAP and Siva-1, confirming that FAIM-L is involved in neuronal plasticity processes through stabilization of XIAP and modulating caspases activity. We have recently characterized an interaction of FAIM-L with tau, a key protein in Alzheimer’s disease, thus showing the relevance of FAIM-L in neurodegenerative processes. In addition, results in mice models show a key role for FAIM-L in retinal homeostasis, by controlling glial response, ubiquitinated protein aggregation, and vascular leakage.
We are now developing new tools to 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 pathologies related with neurodegeneration.
