Bradykinesia in Parkinson's disease may be associated to a dopamine-dependent recruitment failure of subthalamic activity in short bursts of gamma synchrony.
The most common Parkinson’s disease-associated mutation, LRRK2 G2019S, impairs mitophagy in clinically relevant cells within the mouse brain and this defect can be reversed using a novel LRRK2 inhibitor.
Memory over 24 hours was impaired in Parkinson's patients off, rather than on, dopaminergic medication during reinforcement learning, whereas dopamine did not affect positive and negative reinforcement, in contrast to previous studies.
The structure of human PINK1 explains structural regulation and clarity on the impact of loss of function disease-associated mutations, which may stimulate future drug discovery efforts for both familial and idiopathic Parkinson's disease.
Long studied in the context of the central nervous system, LRRK2 also functions in peripheral immunity by maintaining mitochondrial homeostasis in macrophages to regulate the type I interferon response.
Aberrant striatal signaling does not induce drastic changes in the spontaneous discharge rate and pattern of the striatal projection neurons in Parkinson’s disease and Dystonia.
Discovery of a physiological LRRK2 substrate and a new mechanism of Rab regulation should aid Parkinson’s research and the understanding of Rab function.
Pathogenic LRRK2kinase requires Rab10 and RILPL1 to block primary cilia formation, shortening cilia on cholinergic neurons needed for a hedgehog driven circuit that supports dopaminergic neurons in mouse brain.
The alpha-synuclein fibril structure reported here buries residues 50-57 at the interface between its two protofilaments, suggesting that familial Parkinson's disease associated mutations in these residues lead to a structure not compatible with the one presented here.
