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• W2130444809 abstract "LRRK2 is a kinase mutated in Parkinson's disease, but how the protein affects synaptic function remains enigmatic. We identified LRRK2 as a critical regulator of EndophilinA. Using genetic and biochemical studies involving Lrrk loss-of-function mutants and Parkinson-related LRRK2(G2019S) gain-of-kinase function, we show that LRRK2 affects synaptic endocytosis by phosphorylating EndoA at S75, a residue in the BAR domain. We show that LRRK2-mediated EndoA phosphorylation has profound effects on EndoA-dependent membrane tubulation and membrane association in vitro and in vivo and on synaptic vesicle endocytosis at Drosophila neuromuscular junctions in vivo. Our work uncovers a regulatory mechanism that indicates that reduced LRRK2 kinase activity facilitates EndoA membrane association, while increased kinase activity inhibits membrane association. Consequently, both too much and too little LRRK2-dependent EndoA phosphorylation impedes synaptic endocytosis, and we propose a model in which LRRK2 kinase activity is part of an EndoA phosphorylation cycle that facilitates efficient vesicle formation at synapses." @default.
• W2130444809 created "2016-06-24" @default.
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• W2130444809 date "2012-09-01" @default.
• W2130444809 modified "2023-10-15" @default.
• W2130444809 title "LRRK2 Controls an EndoA Phosphorylation Cycle in Synaptic Endocytosis" @default.
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• W2130444809 doi "https://doi.org/10.1016/j.neuron.2012.08.022" @default.
• W2130444809 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22998870" @default.
• W2130444809 hasPublicationYear "2012" @default.
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