Insights into the cellular consequences of LRRK2-mediated Rab protein phosphorylation

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• Insights into the cellular consequences of LRRK2-mediated Rab protein phosphorylation March 17, 2023 Biochem Soc Trans. 2023 Mar 17:BST20201145. doi: 10.1042/BST20201145. Online ahead of print.ABSTRACTPoint mutations in leucine-rich repeat kinase 2 (LRRK2) which cause Parkinson's disease increase its kinase activity, and a subset of Rab GTPases have been identified as endogenous LRRK2 kinase substrates. Their phosphorylation correlates with a loss-of-function for the membrane trafficking steps they are normally involved in, but it also…
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• Insights into the cellular consequences of LRRK2-mediated Rab protein phosphorylation March 17, 2023 Biochem Soc Trans. 2023 Mar 17:BST20201145. doi: 10.1042/BST20201145. Online ahead of print.ABSTRACTPoint mutations in leucine-rich repeat kinase 2 (LRRK2) which cause Parkinson's disease increase its kinase activity, and a subset of Rab GTPases have been identified as endogenous LRRK2 kinase substrates. Their phosphorylation correlates with a loss-of-function for the membrane trafficking steps they are normally involved in, but it also…
• Insights into the cellular consequences of LRRK2-mediated Rab protein phosphorylation March 17, 2023 Biochem Soc Trans. 2023 Mar 17:BST20201145. doi: 10.1042/BST20201145. Online ahead of print.ABSTRACTPoint mutations in leucine-rich repeat kinase 2 (LRRK2) which cause Parkinson's disease increase its kinase activity, and a subset of Rab GTPases have been identified as endogenous LRRK2 kinase substrates. Their phosphorylation correlates with a loss-of-function for the membrane trafficking steps they are normally involved in, but it also…
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