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Article

Structural interface between LRRK2 and 14-3-3 protein.

The Biochemical journal - 23 Mar 2017

Stevers Loes M, de Vries Rens M J M, Doveston Richard G, Milroy Lech-Gustav, Brunsveld Luc, Ottmann Christian

Abstract excerpt

Binding of 14-3-3 proteins to leucine-rich repeat protein kinase 2 (LRRK2) is known to be impaired by many Parkinson's disease (PD)-relevant mutations. Abrogation of this interaction is connected to enhanced LRRK2 kinase activity, which in turn is implicated in increased ubiquitination of LRRK2, accumulation of LRRK2 into inclusion bodies and reduction in neurite length. Hence, the interaction between 14-3-3 and...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Leucine-Rich Repeat Serine-Threonine Protein Kinase-2

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Source

Identifiers

PMID: 28202711
DOI: 10.1042/BCJ20161078

Provenance

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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