LRRK2 autophosphorylation enhances its GTPase activity

Revisiting the Roco G-protein cycle

(2015) Susanne Terheyden et al.   BIOCHEMICAL JOURNAL

LRRK2 delays degradative receptor trafficking by impeding late endosomal budding through decreasing Rab7 activity

(2014) Patricia Gómez-Suaga et al.   HUMAN MOLECULAR GENETICS

The Parkinson Disease-linked LRRK2 Protein Mutation I2020T Stabilizes an Active State Conformation Leading to Increased Kinase Activity

(2014) Soumya Ray et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Unique Functional and Structural Properties of the LRRK2 Protein ATP-binding Pocket

(2014) Zhiyong Liu et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Structural basis for nuclear import of splicing factors by human Transportin 3

(2014) G. N. Maertens et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Parkinson disease-associated mutation R1441H in LRRK2 prolongs the "active state" of its GTPase domain

(2014) J. Liao et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease

(2014) A. Beilina et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Molecular Mechanisms of Phospholipase C β3 Autoinhibition

(2014) Angeline M. Lyon et al.   STRUCTURE

Differential Effects of Familial Parkinson Mutations in LRRK2 Revealed by a Systematic Analysis of Autophosphorylation

(2013) Shogo Kamikawaji et al.   BIOCHEMISTRY

Functional interaction of Parkinson's disease-associated LRRK2 with members of the dynamin GTPase superfamily

(2013) Klodjan Stafa et al.   HUMAN MOLECULAR GENETICS

Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission

(2013) S. Koirala et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Biochemical Characterization of Highly Purified Leucine-Rich Repeat Kinases 1 and 2 Demonstrates Formation of Homodimers

(2012) Laura Civiero et al.   PLoS One

Roco kinase structures give insights into the mechanism of Parkinson disease-related leucine-rich-repeat kinase 2 mutations

(2012) B. K. Gilsbach et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Ser1292 Autophosphorylation Is an Indicator of LRRK2 Kinase Activity and Contributes to the Cellular Effects of PD Mutations

(2012) Z. Sheng et al.   Science Translational Medicine

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

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

The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease

(2010) Mark R. Cookson   NATURE REVIEWS NEUROSCIENCE

Models for the functions of Arf GAPs

(2010) Michael P. East et al.   SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY

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

LRRK2 in Parkinson’s disease: biochemical functions

(2009) Vasanti S. Anand et al.   FEBS Journal

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

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

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

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

Structure of the Roc–COR domain tandem of C. tepidum, a prokaryotic homologue of the human LRRK2 Parkinson kinase

(2008) Katja Gotthardt et al.   EMBO 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

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