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

Mutations in the LRRK2 Roc-COR tandem domain link Parkinson's disease to Wnt signalling pathways.

Human molecular genetics - 15 Oct 2009

Sancho Rosa M, Law Bernard M H, Harvey Kirsten

Abstract excerpt

Mutations in PARK8, encoding LRRK2, are the most common known cause of Parkinson's disease. The LRRK2 Roc-COR tandem domain exhibits GTPase activity controlling LRRK2 kinase activity via an intramolecular process. We report the interaction of LRRK2 with the dishevelled family of phosphoproteins (...

Read the complete abstract on PubMed

Topics

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

Share to Adaptor Proteins, Signal Transducing
Share to Dishevelled Proteins
Share to Leucine-Rich Repeat Serine-Threonine Protein Kinase-2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Parkinson Disease

Share to Phosphoproteins

Share to Protein Serine-Threonine Kinases

Share to Protein Structure, Tertiary

Share to Wnt Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 19625296
DOI: 10.1093/hmg/ddp337
PMCID: PMC2748899

Genes

DVL1

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19625296-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations in the LRRK2 Roc-COR tandem domain link Parkinson's disease to Wnt signalling pathways.PMID 19625296Read ↗

A proteomic analysis of LRRK2 binding partners reveals interactions with multiple signaling components of the WNT/PCP pathway.Semantic proximity Read ↗

LRRK2 functions as a Wnt signaling scaffold, bridging cytosolic proteins and membrane-localized LRP6.Semantic proximity Read ↗

The Parkinson Disease Gene LRRK2: Evolutionary and Structural InsightsSemantic proximity Read ↗

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

The Parkinson’s Disease-Associated Protein Kinase LRRK2 Modulates Notch Signaling through the Endosomal PathwaySemantic proximity Read ↗

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

Leucine-rich repeat kinase 2: relevance to Parkinson's disease.Semantic proximity Read ↗

Contribution of GTPase activity to LRRK2-associated Parkinson disease.Semantic proximity Read ↗

Dysregulated Wnt and NFAT signaling in a Parkinson's disease LRRK2 G2019S knock-in model.Semantic proximity Read ↗

Insight into the mode of action of the LRRK2 Y1699C pathogenic mutant.Semantic proximity Read ↗

Structural biology of the LRRK2 GTPase and kinase domains: implications for regulationSemantic proximity Read ↗

LRRK1 protein kinase activity is stimulated upon binding of GTP to its Roc domain.Semantic proximity Read ↗

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