GTPase activity regulates kinase activity and cellular phenotypes of Parkinson's disease-associated LRRK2

The G2385R variant of leucine-rich repeat kinase 2 associated with Parkinson's disease is a partial loss-of-function mutation

(2012) Iakov N. Rudenko et al.   BIOCHEMICAL JOURNAL

Mechanisms of LRRK2-Mediated Neurodegeneration

(2012) Elpida Tsika et al.   Current Neurology and Neuroscience Reports

ArfGAP1 Is a GTPase Activating Protein for LRRK2: Reciprocal Regulation of ArfGAP1 by LRRK2

(2012) Y. Xiong et al.   JOURNAL OF NEUROSCIENCE

GTPase Activity and Neuronal Toxicity of Parkinson's Disease–Associated LRRK2 Is Regulated by ArfGAP1

(2012) Klodjan Stafa et al.   PLoS Genetics

Chemoproteomics-Based Design of Potent LRRK2-Selective Lead Compounds That Attenuate Parkinson’s Disease-Related Toxicity in Human Neurons

(2011) Nigel Ramsden et al.   ACS Chemical Biology

Structure-Function Relationships of the G Domain, a Canonical Switch Motif

(2011) Alfred Wittinghofer et al.   Annual Review of Biochemistry

Re-examination of the dimerization state of leucine-rich repeat kinase 2: predominance of the monomeric form

(2011) Genta Ito et al.   BIOCHEMICAL JOURNAL

LRRK2 protein levels are determined by kinase function and are crucial for kidney and lung homeostasis in mice

(2011) Martin C. Herzig et al.   HUMAN MOLECULAR GENETICS

Autophosphorylation in the Leucine-Rich Repeat Kinase 2 (LRRK2) GTPase Domain Modifies Kinase and GTP-Binding Activities

(2011) Philip J. Webber et al.   JOURNAL OF MOLECULAR BIOLOGY

A Rat Model of Progressive Nigral Neurodegeneration Induced by the Parkinson's Disease-Associated G2019S Mutation in LRRK2

(2011) J. Dusonchet et al.   JOURNAL OF NEUROSCIENCE

LRRK2 Kinase Activity Is Dependent on LRRK2 GTP Binding Capacity but Independent of LRRK2 GTP Binding

(2011) Jean-Marc Taymans et al.   PLoS One

Membrane Localization of LRRK2 Is Associated with Increased Formation of the Highly Active LRRK2 Dimer and Changes in Its Phosphorylation

(2010) Zdenek Berger et al.   BIOCHEMISTRY

Phosphopeptide Analysis Reveals Two Discrete Clusters of Phosphorylation in the N-Terminus and the Roc Domain of the Parkinson-Disease Associated Protein Kinase LRRK2

(2010) Christian Johannes Gloeckner et al.   JOURNAL OF PROTEOME RESEARCH

GTPase Activity Plays a Key Role in the Pathobiology of LRRK2

(2010) Yulan Xiong et al.   PLoS Genetics

The Parkinson’s disease kinase LRRK2 autophosphorylates its GTPase domain at multiple sites

(2009) Elisa Greggio et al.   BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS

Identification of the Autophosphorylation Sites of LRRK2

(2009) Shogo Kamikawaji et al.   BIOCHEMISTRY

Dependence of Leucine-rich Repeat Kinase 2 (LRRK2) Kinase Activity on Dimerization

(2009) Saurabh Sen et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Phosphorylation of Ezrin/Radixin/Moesin Proteins by LRRK2 Promotes the Rearrangement of Actin Cytoskeleton in Neuronal Morphogenesis

(2009) L. Parisiadou et al.   JOURNAL OF NEUROSCIENCE

It takes two to tango: regulation of G proteins by dimerization

(2009) Raphael Gasper et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

The Roco protein family: a functional perspective

(2008) Ignacio Marín et al.   FASEB JOURNAL

The Parkinson Disease-associated Leucine-rich Repeat Kinase 2 (LRRK2) Is a Dimer That Undergoes Intramolecular Autophosphorylation

(2008) Elisa Greggio et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Role of autophagy in G2019S-LRRK2-associated neurite shortening in differentiated SH-SY5Y cells

(2008) Edward D. Plowey et al.   JOURNAL OF NEUROCHEMISTRY

Phenotype, genotype, and worldwide genetic penetrance of LRRK2-associated Parkinson's disease: a case-control study

(2008) Daniel G Healy et al.   LANCET NEUROLOGY

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

(2008) J. Deng et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA