Associated Papers
Structural basis for binding of RILPL1 to TMEM55B reveals a lysosomal platform for adaptor assembly through a conserved peptide motif.
Waschbüsch D et al.
Structure (london, England : 1993), 2026
Functional and Structural Characterization of LRRK2 p.V1447L in Parkinson's Disease.
Pratuseviciute N et al.
Movement Disorders : Official Journal of the Movement Disorder Society, 2025
Structural basis for binding of RILPL1 to TMEM55B reveals a lysosomal platform for adaptor assembly through a conserved TBM motif.
Waschbüsch D et al.
Biorxiv : the Preprint Server for Biology, 2025
Lysosomal TPC2 channels disrupt Ca2+ entry and dopaminergic function in models of LRRK2-Parkinson's disease.
Gregori M et al.
The Journal of Cell Biology, 2025
Clinical and functional evidence for the pathogenicity of the LRRK2 p.Arg1067Gln variant.
Lim SY et al.
Npj Parkinson's Disease, 2025
Upregulated ECM genes and increased synaptic activity in Parkinson's human DA neurons with PINK1/ PRKN mutations.
Tripathi U et al.
Npj Parkinson's Disease, 2024
RedOx regulation of LRRK2 kinase activity by active site cysteines.
Trilling CR et al.
Npj Parkinson's Disease, 2024
Parkinson's VPS35[D620N] mutation induces LRRK2-mediated lysosomal association of RILPL1 and TMEM55B.
Pal P et al.
Science Advances, 2023
Genome-wide screen reveals Rab12 GTPase as a critical activator of Parkinson's disease-linked LRRK2 kinase.
Dhekne HS et al.
Elife, 2023
Endogenous Rab38 regulates LRRK2's membrane recruitment and substrate Rab phosphorylation in melanocytes.
Unapanta A et al.
The Journal of Biological Chemistry, 2023
Novel LRR-ROC Motif That Links the N- and C-terminal Domains in LRRK2 Undergoes an Order-Disorder Transition Upon Activation.
Weng JH et al.
Journal of Molecular Biology, 2023
Capturing the domain crosstalk in full length LRRK2 and LRRK2RCKW.
Störmer E et al.
The Biochemical Journal, 2023
PKC isoforms activate LRRK1 kinase by phosphorylating conserved residues (Ser1064, Ser1074 and Thr1075) within the CORB GTPase domain.
Malik AU et al.
The Biochemical Journal, 2022
A feed-forward pathway drives LRRK2 kinase membrane recruitment and activation.
Vides EG et al.
Elife, 2022
Impact of 100 LRRK2 variants linked to Parkinson's disease on kinase activity and microtubule binding.
Kalogeropulou AF et al.
The Biochemical Journal, 2022
Conformation and dynamics of the kinase domain drive subcellular location and activation of LRRK2.
Schmidt SH et al.
Proceedings of the National Academy of Sciences of the United States of America, 2021
Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms.
Malik AU et al.
The Biochemical Journal, 2021
Origins of Parkinson's Disease in Brain Development: Insights From Early and Persistent Effects of LRRK2-G2019S on Striatal Circuits.
Huntley GW et al.
Frontiers in Neuroscience, 2020
LRRK2 Phosphorylation, More Than an Epiphenomenon.
Marchand A et al.
Frontiers in Neuroscience, 2020
Progress in LRRK2-Associated Parkinson's Disease Animal Models.
Seegobin SP et al.
Frontiers in Neuroscience, 2020
Membrane association but not identity is required for LRRK2 activation and phosphorylation of Rab GTPases.
Gomez RC et al.
The Journal of Cell Biology, 2019
The dynamic switch mechanism that leads to activation of LRRK2 is embedded in the DFGψ motif in the kinase domain.
Schmidt SH et al.
Proceedings of the National Academy of Sciences of the United States of America, 2019
Leucine-rich repeat kinase 2 (LRRK2) inhibitors differentially modulate glutamate release and Serine935 LRRK2 phosphorylation in striatal and cerebrocortical synaptosomes.
Mercatelli D et al.
Pharmacology Research & Perspectives, 2019
Crystal structure of the WD40 domain dimer of LRRK2.
Zhang P et al.
Proceedings of the National Academy of Sciences of the United States of America, 2019
Functional and behavioral consequences of Parkinson's disease-associated LRRK2-G2019S mutation.
Benson DL et al.
Biochemical Society Transactions, 2018
Lrrk promotes tau neurotoxicity through dysregulation of actin and mitochondrial dynamics.
Bardai FH et al.
Plos Biology, 2018
P62/SQSTM1 is a novel leucine-rich repeat kinase 2 (LRRK2) substrate that enhances neuronal toxicity.
Kalogeropulou AF et al.
The Biochemical Journal, 2018
Rab29 activation of the Parkinson's disease-associated LRRK2 kinase.
Purlyte E et al.
The Embo Journal, 2018
Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation establishes a connection to ciliogenesis.
Steger M et al.
Elife, 2017
LRRK2 promotes the activation of NLRC4 inflammasome during Salmonella Typhimurium infection.
Liu W et al.
The Journal of Experimental Medicine, 2017
Pathogenic LRRK2 variants are gain-of-function mutations that enhance LRRK2-mediated repression of β-catenin signaling.
Berwick DC et al.
Molecular Neurodegeneration, 2017
A LRRK2-Dependent EndophilinA Phosphoswitch Is Critical for Macroautophagy at Presynaptic Terminals.
Soukup SF et al.
Neuron, 2016
'Up with the LRRK': a phosphorylated Rab10 assay for evaluation of LRRK2 activity and inhibitor engagement.
Eyers PA
The Biochemical Journal, 2016
Phos-tag analysis of Rab10 phosphorylation by LRRK2: a powerful assay for assessing kinase function and inhibitors.
Ito G et al.
The Biochemical Journal, 2016
Altered Development of Synapse Structure and Function in Striatum Caused by Parkinson's Disease-Linked LRRK2-G2019S Mutation.
Matikainen-Ankney BA et al.
The Journal of Neuroscience : the Official Journal of the Society for Neuroscience, 2016
LRRK2 Promotes Tau Accumulation, Aggregation and Release.
Guerreiro PS et al.
Molecular Neurobiology, 2016
Arsenite stress down-regulates phosphorylation and 14-3-3 binding of leucine-rich repeat kinase 2 (LRRK2), promoting self-association and cellular redistribution.
Mamais A et al.
The Journal of Biological Chemistry, 2014
Prediction of the repeat domain structures and impact of parkinsonism-associated variations on structure and function of all functional domains of leucine-rich repeat kinase 2 (LRRK2).
Mills RD et al.
Human Mutation, 2014
Lack of correlation between the kinase activity of LRRK2 harboring kinase-modifying mutations and its phosphorylation at Ser910, 935, and Ser955.
Ito G et al.
Plos One, 2014