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Using cryo-EM, biochemical reconstitution, and cell-based assays, it is shown that the ROC GTPase governs switching between autoinhibited and active states: GTP binding promotes activation, whereas GDP binding enforces autoinhibition.
This study utilizes a chemical genetic approach to sensitize LRRK2 to existing GTPase inhibitors and shows that pharmacologically engaging the Roc-COR GTPase domain in cells decreases but does not fully inhibit LRRK2-mediated Rab10 T73 phosphorylation.
A unified framework for understanding LRRK2 regulation with broad therapeutic implications is provided, showing that the ROC GTPase governs switching between autoinhibited and active states: GTP binding promotes activation, whereas GDP binding enforces autoinhibition.
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