Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Nature communications - 5 Aug 2025

Martinez Fiesco Juliana A, Beilina Alexandra, Alvarez de la Cruz Astrid, Li Ning, Metcalfe Riley D, Cookson Mark R, Zhang Ping

Abstract excerpt

Leucine-rich repeat kinase 2 (LRRK2) is an essential regulator in cellular signaling and a major contributor to Parkinson's disease (PD) pathogenesis. 14-3-3 proteins are critical modulators of LRRK2 activity, yet the structural basis of their interaction has remained unclear. Here, we present the cryo-electron microscopy structure of the LRRK2:14-3-32 autoinhibitory complex, revealing how a 14-3-3 dimer...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to 14-3-3 Proteins
Share to Cryoelectron Microscopy

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to HEK293 Cells

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

Share to Parkinson Disease

Share to Phosphorylation

Share to Protein Domains

Share to Protein Multimerization

Source

Open in PubMed Open full text

Identifiers

PMID: 40764514
DOI: 10.1038/s41467-025-62337-1
PMCID: PMC12325948

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 24 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

14-3-3 binding maintains the Parkinson's associated kinase LRRK2 in an inactive state.PMID 40764514Read ↗

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

Structural model of the dimeric Parkinson's protein LRRK2 reveals a compact architecture involving distant interdomain contacts.Semantic proximity Read ↗

Conformation and dynamics of the kinase domain drive subcellular location and activation of LRRK2Semantic proximity Read ↗

The structural basis for LRRK2’s activation and autoinhibitionSemantic proximity Read ↗

Structure of LRRK1 and mechanisms of autoinhibition and activationSemantic proximity Read ↗

Structure of LRRK1 and mechanisms of autoinhibition and activation.Semantic proximity Read ↗

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

Structural and biochemical basis of ROC-dependent activation of LRRK2Semantic proximity Read ↗

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

LRRK2 Structure-Based Activation Mechanism and Pathogenesis.Semantic proximity Read ↗

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

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

⌁Select a neighboring publication to make it the new centre.