The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Phosphorylation of Ezrin/Radixin/Moesin Proteins by LRRK2 Promotes the Rearrangement of Actin Cytoskeleton in Neuronal Morphogenesis
Open accessAbstract
Leucine-rich repeat kinase 2 (LRRK2) functions as a putative protein kinase of ezrin, radixin, and moesin (ERM) family proteins. A Parkinson's disease-related G2019S substitution in the kinase domain of LRRK2 further enhances the phosphorylation of ERM proteins. The phosphorylated ERM (pERM) proteins are restricted to the filopodia of growing neurites in which they tether filamentous actin (F-actin) to the cytoplasmic membrane and regulate the dynamics of filopodia protrusion. Here, we show that, in cultured neurons derived from LRRK2 G2019S transgenic mice, the number of pERM-positive and F-actin-enriched filopodia was significantly increased, and this correlates with the retardation of neurite outgrowth. Conversely, deletion of LRRK2, which lowered the pERM and F-actin contents in filopodia, promoted neurite outgrowth. Furthermore, inhibition of ERM phosphorylation or actin polymerization rescued the G2019S-dependent neuronal growth defects. These data support a model in which the G2019S mutation of LRRK2 causes a gain-of-function effect that perturbs the homeostasis of pERM and F-actin in sprouting neurites critical for neuronal morphogenesis.
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Citations
Cites
Mutations in LRRK2 Cause Autosomal-Dominant Parkinsonism with Pleomorphic Pathology
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Cloning of the Gene Containing Mutations that Cause PARK8-Linked Parkinson's Disease
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ERM proteins and merlin: integrators at the cell cortex
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Parkinson's disease-associated mutations in leucine-rich repeat kinase 2 augment kinase activity
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Kinase activity is required for the toxic effects of mutant LRRK2/dardarin
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Kinase activity of mutant LRRK2 mediates neuronal toxicity
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Cited by
Clinical progression in Parkinson disease and the neurobiology of axons
Cheng, H., Ulane, C. M., & Burke, R. E. (2010) · Annals of Neurology · doi:10.1002/ana.21995 · Cited by 1,012
“Similar observations were made for the LRRK2(G2019S) mutant in neuronally differentiated neuroblastoma cells(45) and in primary neurons derived from transgenic mice.(46) The molecular basis of these effects is not known, but of potential interest in this regard is the identification of moesin, and the closely allied p…”
BackgroundResultAxon degeneration in Parkinson's disease
Burke, R. E., & O'Malley, K. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2012.01.011 · Cited by 493
Genetics in Parkinson disease: Mendelian versus non‐Mendelian inheritance
Hernandez, D. G., Reed, X., & Singleton, A. B. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13593 · Cited by 448
“…autophagy, cytoskeletal dynamics, kinase cascades, mitochondrial function, and vesicular trafficking (MacLeod et al. 2006; Gloeckner et al. 2009; Parisiadou et al. 2009;Mortiboys et al. 2010; Niu et al. 2012; Bravo-San Pedro et al. 2013; Manzoni et al. 2013; Orenstein et al. 2013; Beilina et…”
BackgroundLRRK2 Inhibition Attenuates Microglial Inflammatory Responses
Moehle, M. S., Webber, P. J., Tse, T., Sukar, N., Standaert, D. G., DeSilva, T. M., Cowell, R. M., & West, A. B. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5601-11.2012 · Cited by 463
Recent Advances in the Genetics of Parkinson's Disease
Martin, I., Dawson, V. L., & Dawson, T. M. (2011) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-082410-101440 · Cited by 437
Metadata
- Authors
- Parisiadou, L., Xie, C., Cho, H. J., Lin, X., Gu, X.-L., Long, C.-X., Lobbestael, E., Baekelandt, V., Taymans, J.-M., Sun, L., & Cai, H.
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2009-11-04
- Volume
- 29
- Issue
- 44
- Pages
- 13971-13980
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- OpenAlex
- W2113282929
- Cited by
- 306
- References
- 36
- FWCI
- 16.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Phosphorylation of Ezrin/Radixin/Moesin Proteins by LRRK2 Promotes the Rearrangement of Actin Cytoskeleton in Neuronal Morphogenesis. https://app.cochat.ai/papers/10.1523/jneurosci.3799-09.2009
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- Parisiadou, L., Xie, C., Cho, H. J., Lin, X., Gu, X.-L., Long, C.-X., Lobbestael, E., Baekelandt, V., Taymans, J.-M., Sun, L., & Cai, H. (2009). Phosphorylation of Ezrin/Radixin/Moesin Proteins by LRRK2 Promotes the Rearrangement of Actin Cytoskeleton in Neuronal Morphogenesis. The Journal of Neuroscience. https://doi.org/10.1523/jneurosci.3799-09.2009
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
