In 2005 I obtained my PhD in Molecular Physiology at University of Padova in collaboration with the National Institute of Health (Bethesda, USA) in Mark Cookson’s laboratory, which I joined for my postdoctoral training until 2009, when I returned to University of Padova with a Brain Gain Assistant Professorship. Since 2014, I am Associate Professor at the University of Padova and Coordinator of the Physiology, Genetic and Behavior Unit. My research is centered around the understanding of the molecular mechanisms leading to neurodegeneration in Parkinson’s disease and related disorders. My major contribution in the field has been the characterization of the pathobiology of LRRK2 at molecular, cellular and organismal level. I was the first to establish the role of LRRK2 kinase activity in neurodegeneration (Greggio et al., 2006), setting the stage for prolific research on LRRK2 inhibitors as Parkinson’s therapeutics. Thanks to the support from Michael J Fox and Telethon grants, my team discovered the protective nature of PAK6 against LRRK2-linked PD, disclosed novel roles of LRRK2 at the presynaptic compartment and contributed to the understanding of LRRK2 in neuroinflammation. My group also investigates the pathobiology of SPG11/spatacsin, a protein mutated in a familiar form of Hereditary Spastic Paraplegia with parkinsonism and of the lysosomal enzyme GBA1, whose mutations confer risk for Parkinson. I participated to several collaborative projects bringing unique expertise in PD biology and coordinated six international grants. I was invited to present my work 26 times as seminars (notably at Oxford University and UCL), lectures at symposia and conference talks. I organized two Biochemical Society Focused meetings on LRRK2 (2016 and 2018). I published 87 papers with h-index of 37 / 46 (Scopus / Google Scholar).

My laboratory is interested in studying the molecular mechanisms underlying the early events of neurodegeneration associated with Parkinson’s disease. We are particularly focused on the pathophysiology of the kinase LRRK2, whose mutations represent the single most common cause of familial Parkinson’s disease, on glucocerebrosidase (GBA), a lysosomal enzyme that mutated represents the most important risk factor for Parkinson's disease, and on SPG11, a lysosomal protein mutated in a familial form of Hereditary Spastic Paraplegia with parkinsonism. We combine cellular and animal models to investigate the signaling pathways and the pathological consequences of gene mutations on neuronal and glial cells homeostasis.

1. Role of the Parkinson’s disease kinase LRRK2 in shaping neurites and synapses 2. Neuronal signalling associated with the kinase PAK6 3. Role of 14-3-3 proteins in the neuronal regulation of TFEB, the master coordinator of autophagy and lysosome biogenesis 4. Role of SPG11, a protein mutated in Hereditary Spastic Paraplegia, in the autophagy-lysosomal pathway 5. Regulation of GBA activity, subcellular localization and lysosomal function by LRRK2