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Article

14-3-3 proteins are promising LRRK2 interactors.

The Biochemical journal - 15 Sept 2010

Rudenko Iakov N, Cookson Mark R

Abstract excerpt

Mutations in LRRK2 (leucine-rich repeat kinase 2) are the most common cause of familial PD (Parkinson's disease). Mutations that cause PD are found in either the GTPase or kinase domains of LRRK2 or an intervening sequence called the COR [C-terminus of ROC (Ras of complex proteins)] domain. As well as the two catalytic domains, LRRK2 possesses several protein-protein interaction domains, but their function and...

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Source

Identifiers

PMID: 20795948
DOI: 10.1042/BJ20101200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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14-3-3 proteins are promising LRRK2 interactors.PMID 20795948Read ↗

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 ↗

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

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

Activation Mechanism of LRRK2 and Its Cellular Functions in Parkinson’s DiseaseSemantic proximity Read ↗

Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPaseSemantic proximity Read ↗

Binding of the Human 14-3-3 Isoforms to Distinct Sites in the Leucine-Rich Repeat Kinase 2Semantic 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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LRRK1 protein kinase activity is stimulated upon binding of GTP to its Roc domain.Semantic proximity Read ↗

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