Synucleinopathies (e.g. Parkinson's disease and dementia with Lewy bodies) are neurodegenerative conditions characterized by an accumulation of alpha-synuclein from the prodromal phase. Yet, the pathophysiology is far from being completely understood. We have recently identified the cortical synaptic depletion of eukaryotic elongation factor 1A proteins (EEF1A) at early stages of the disease in a mouse model of synucleinopathy (human alpha-synuclein expressing animals under PDGF promoter specific to various brain tissues, PDGF-hSyn).In order to link EEF1A proteins to synucleinopathy changes, we analyzed the time course of EEF1A1/ EEF1A2 variant loss in a PDGF-hSyn mouse model. Furthermore, we successfully developed a CRISPR/Cas9-mediated strategies for fluorescent endogenous EEF1A/EEF1A2 protein tagging for assessment of neuronal synucleinopathy-related differences and precise neuronal localization of the EEF1A variants.EEF1A proteins conduct different roles in the cell. While they are predominantly involved in protein translation functions, they are also crucial players in actin bundling, cell death and misfolded protein degradation. We aim at exploring these functions of EEF1A proteins in PDGF-hSyn animals and study the EEF1A proteins involvement by their genetic and pharmacological modulation.Our work will unravel the function of EEF1A at synapses and provide characterization of its implication in the pathophysiology of synucleinopathy.