Article ID Journal Published Year Pages File Type
10871497 FEBS Letters 2011 6 Pages PDF
Abstract
► We found that LRRK2 directly phosphorylated Akt1 at Ser473. ► The knockdown of LRRK2 resulted in a marked reduction of phospho-Akt1 at Ser473. ► The R1441C, G2019S, and I2020T mutant LRRK2 exhibited reduced interaction with, and phosphorylation of, Akt1. ► Akt1 is one of the physiological substrates of LRRK2.
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Life Sciences Agricultural and Biological Sciences Plant Science
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LRRK2 directly phosphorylates Akt1 as a possible physiological substrate: Impairment of the kinase activity by Parkinson's disease-associated mutations
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