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Article

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

Human molecular genetics - 20 Nov 2024

Pattanayak Rudradip, Ekkatine Roschongporn, Petit Chad M, Yacoubian Talene A

Abstract excerpt

LRRK2 mutations are among the most common genetic causes for Parkinson's disease (PD), and toxicity is associated with increased kinase activity. 14-3-3 proteins are key interactors that regulate LRRK2 kinase activity. Phosphorylation of the 14-3-3θ isoform at S232 is dramatically increased in human PD brains. Here we investigate the impact of 14-3-3θ phosphorylation on its ability to regulate LRRK2 kinase...

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Identifiers

PMID: 39324210
DOI: 10.1093/hmg/ddae142
PMCID: PMC11578116

Provenance

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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14-3-3 phosphorylation inhibits 14-3-3θ's ability to regulate LRRK2 kinase activity and toxicity.PMID 39324210Read ↗

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

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

14-3-3 Proteins regulate mutant LRRK2 kinase activity and neurite shortening.Semantic proximity Read ↗

14-3-3 binding maintains the Parkinson’s associated kinase LRRK2 in an inactive stateSemantic proximity Read ↗

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

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

Structural interface between LRRK2 and 14-3-3 protein.Semantic proximity Read ↗

Binding of the Human 14-3-3 Isoforms to Distinct Sites in the Leucine-Rich Repeat Kinase 2Semantic proximity Read ↗

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

Pathways to Parkinson’s disease: a spotlight on 14-3-3 proteinsSemantic proximity Read ↗

Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins.Semantic proximity Read ↗

Parkinson-related LRRK2 mutation R1441C/G/H impairs PKA phosphorylation of LRRK2 and disrupts its interaction with 14-3-3.Semantic proximity Read ↗

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