The R1441C mutation of LRRK2 disrupts GTP hydrolysis.

doi:10.1016/j.bbrc.2007.04.006

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Article

The R1441C mutation of LRRK2 disrupts GTP hydrolysis.

Biochemical and biophysical research communications - 8 Jun 2007

Lewis Patrick A, Greggio Elisa, Beilina Alexandra, Jain Shushant, Baker Acacia, Cookson Mark R

Abstract excerpt

Mutations in Leucine Rich Repeat Kinase 2 (LRRK2) are the leading genetic cause of Parkinson's disease (PD). LRRK2 is predicted to contain kinase and GTPase enzymatic domains, with recent evidence suggesting that the kinase activity of LRRK2 is central to the pathogenic process associated with this protein. The GTPase domain of LRRK2 plays an important role in the regulation of kinase activity. To investigate how...

Topics

Amino Acid Substitution
Animals
COS Cells
Chlorocebus aethiops
GTP Phosphohydrolases
Guanosine Diphosphate
Guanosine Triphosphate
Humans
Hydrolysis
Immunoblotting
Immunoprecipitation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Kinetics

Leucine-Rich Repeat Serine-Threonine Protein Kinase-2

Mutation

Parkinson Disease

Protein Binding

Protein Serine-Threonine Kinases

Source

Open in PubMed Open full text

Identifiers

PMID: 17442267
DOI: 10.1016/j.bbrc.2007.04.006
PMCID: PMC1939973

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-17442267-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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