Leucine-rich repeat kinase 2 (LRRK2) is a large serine-threonine kinase of 2527 aminoacids. Five mutations in the LRRK2 gene account for the majority of genetic Parkinson's disease (PD) cases. This pathology is characterized by the progressive death of the neurons of the substantia nigra pars compacta, which have been related to the observed movement disorders (tremor, bradykinesia, rigidity). The physiological functions of LRRK2 are still not known, but LRRK2 murine models show defects in neurotransmission. We have recently demonstrated the involvement of this protein at the presynaptic site. In particular, the absence of LRRK2 decreases the number of docked vesicles, increases the mobility of synaptic vesicles trafficking and the evoked post-synaptic currents. Pull-down assays have shown that LRRK2 via its WD40 C-terminal domain interacts with several presynaptic proteins, among which N-ethylmaleimide sensitive fusion protein (NSF), synapsin I, clathrin and AP-2 subunits and, interestingly, the physiological function of these proteins is modulated by phosphorylation. Here, we show that LRRK2 phosphorylates in vitro NSF, an homohexameric AAA+ ATPase responsible of the disassembling of SNARE complex. We are currently identifying the phosphosite/s and unraveling the physiological effects of this phosphorylation on the ATPase activity and oligomerization of NSF.