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Article

Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization.

The Biochemical journal - 15 Sept 2010

Dzamko Nicolas, Deak Maria, Hentati Faycal, Reith Alastair D, Prescott Alan R, Alessi Dario R, Nichols R Jeremy

Abstract excerpt

LRRK2 (leucine-rich repeat protein kinase 2) is mutated in a significant number of Parkinson's disease patients. Since a common mutation that replaces Gly2019 with a serine residue enhances kinase catalytic activity, small-molecule LRRK2 inhibitors might have utility in treating Parkinson's disease. However, the effectiveness of inhibitors is difficult to assess, as no physiological substrates or downstream...

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Identifiers

PMID: 20659021
DOI: 10.1042/BJ20100784
PMCID: PMC3631100

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization.PMID 20659021Read ↗

14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization.Semantic proximity Read ↗

Phosphorylation-dependent 14-3-3 binding to LRRK2 is impaired by common mutations of familial Parkinson's disease.Semantic proximity Read ↗

14-3-3 phosphorylation inhibits 14-3-3θ's ability to regulate LRRK2 kinase activity and toxicity.Semantic proximity Read ↗

Measurement of LRRK2 and Ser910/935 phosphorylated LRRK2 in peripheral blood mononuclear cells from idiopathic Parkinson's disease patients.Semantic proximity Read ↗

14-3-3 phosphorylation inhibits 14-3-3θ’s ability to regulate LRRK2 kinase activitySemantic proximity Read ↗

An Assessment of LRRK2 Serine 935 Phosphorylation in Human Peripheral Blood Mononuclear Cells in Idiopathic Parkinson’s Disease and G2019S LRRK2 CohortsSemantic proximity Read ↗

LRRK2 exonic variants associated with Parkinson’s disease augment phosphorylation levels for LRRK2-Ser1292 and Rab10-Thr73Semantic proximity Read ↗

Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease.Semantic proximity Read ↗

14-3-3 binding maintains the Parkinson's associated kinase LRRK2 in an inactive state.Semantic proximity Read ↗

Unique functional and structural properties of the LRRK2 protein ATP-binding pocket.Semantic proximity Read ↗

LRRK2 phosphorylation status and kinase activity regulate (macro)autophagy in a Rab8a/Rab10-dependent manner.Semantic proximity Read ↗

Impact of Type II LRRK2 inhibitors on signalling and mitophagySemantic proximity Read ↗

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