ArticleJournal of neuroscience research2008
The Roc domain of leucine-rich repeat kinase 2 is sufficient for interaction with microtubules.
Article in Journal of neuroscience research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
86 citing papers in PubMed, 169 citations in OpenAlex.
- Recent advances in targeting LRRK2 for Parkinson's disease treatment.Journal of translational medicine · 2025Review
- Loss of LRRK2 activity induces cytoskeleton defects and oxidative stress during porcine oocyte maturation.Cell communication and signaling : CCS · 2025Article
- Genetic evidence for a functional association between Parkinson's disease proteins leucine-rich repeat kinase 2 andFrontiers in molecular neuroscience · 2025Article
- VP28 interacts with PmRab7 irrespective of its nucleotide state.Scientific reports · 2024Article
- Rare variants with large effects provide functional insights into the pathology of migraine subtypes, with and without aura.Nature genetics · 2023Article
- Human Induced Pluripotent Stem Cell Phenotyping and Preclinical Modeling of Familial Parkinson's Disease.Genes · 2022Review
- The E3 ligase TRIM1 ubiquitinates LRRK2 and controls its localization, degradation, and toxicity.The Journal of cell biology · 2022Article
- Astrocytic atrophy as a pathological feature of Parkinson's disease with LRRK2 mutation.NPJ Parkinson's disease · 2021Article
- Microtubule Dysfunction: A Common Feature of Neurodegenerative Diseases.International journal of molecular sciences · 2020Review
- The pseudoGTPase group of pseudoenzymes.The FEBS journal · 2020Review
- Article
- WD40-Repeat Proteins in Ciliopathies and Congenital Disorders of Endocrine System.Endocrinology and metabolism (Seoul, Korea) · 2020Review
- Proteomics; applications in familial Parkinson's disease.Journal of neurochemistry · 2019Review
- Functional Segments on Intrinsically Disordered Regions in Disease-Related Proteins.Biomolecules · 2019Article
- Roco Proteins: GTPases with a Baroque Structure and Mechanism.International journal of molecular sciences · 2019Review
- LRRK2 and mitochondria: Recent advances and current views.Brain research · 2019Review
- Roco Proteins and the Parkinson's Disease-Associated LRRK2.International journal of molecular sciences · 2018Review
- The Small GTPase RAC1/CED-10 Is Essential in Maintaining Dopaminergic Neuron Function and Survival Against α-Synuclein-Induced Toxicity.Molecular neurobiology · 2018Article
- Potential for therapeutic targeting of AKAP signaling complexes in nervous system disorders.Pharmacology & therapeutics · 2018Review
- Targeted Next-generation Sequencing and Bioinformatics Pipeline to Evaluate Genetic Determinants of Constitutional Disease.Journal of visualized experiments : JoVE · 2018Article
26 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Mutations in the leucine-rich repeat kinase 2 (LRRK2) gene are the leading cause of genetically inherited Parkinson's disease (PD). Although this multidomain protein has been shown to have both GTPase and kinase activities through the Roc and MAPKKK domains, respectively, the protein-protein interactions and pathways involved in LRRK2-mediated signaling remain elusive. Utilizing a combination of protein pull-down assays, mass spectrometry, Western blotting, and immunofluorescence microscopy, this study identifies and describes the interaction between LRRK2 and microtubules. The Roc or GTPase-like domain of LRRK2 is sufficient for interaction with alpha/beta-tubulin heterodimers. This interaction occurs in a guanine nucleotide-independent manner, suggesting that tubulin might not be an effector of the LRRK2 GTPase domain. The R1441C pathogenic mutation, located within the Roc domain, retains interaction with alpha/beta-tubulin heterodimers, suggesting that disruption of this interaction likely is not the mechanism whereby the R1441C mutation leads to disease. At a subcellular level, endogenous LRRK2 protein was found to colocalize with alpha/beta-tubulin in primary hippocampal neurons. These findings are significant in that they link LRRK2 with microtubules, a structural component of the cell that is critically involved in the pathogenesis of several neurodegenerative diseases, including PD.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.