ArticleProceedings of the National Academy of Sciences of the United States of America2023
Membrane remodeling properties of the Parkinson's disease protein LRRK2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Targeting of kinases to treat neurodegenerative diseases.Pharmacological reviews · 2026Review
- Article
- Article
- Cryo-electron tomography reveals the microtubule-bound form of inactive LRRK2.bioRxiv : the preprint server for biology · 2025Article
- Salmonella exploits LRRK2-dependent plasma membrane dynamics to invade host cells.Nature communications · 2025Article
- The spectrum of lysosomal stress and damage responses: from mechanosensing to inflammation.EMBO reports · 2025Review
- A STING-CASM-GABARAP pathway activates LRRK2 at lysosomes.The Journal of cell biology · 2025Article
- Galactocerebroside Lipid Nanotubes, a Model Membrane System for Studying Membrane-Associated Proteins on a Molecular Scale.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Plasma membrane curvature regulates the formation of contacts with the endoplasmic reticulum.Nature cell biology · 2024Article
- Mechanisms of lysosomal tubulation and sorting driven by LRRK2.Biochemical Society transactions · 2024Review
- Membrane Curvature Promotes ER-PM Contact Formation via Junctophilin-EHD Interactions.bioRxiv : the preprint server for biology · 2024Article
- Protein-membrane interactions: sensing and generating curvature.Trends in biochemical sciences · 2024Review
- Membrane remodeling properties of the Parkinson's disease protein LRRK2.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- LRRK2 suppresses lysosome degradative activity in macrophages and microglia through MiT-TFE transcription factor inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
Abstract
Mutations in Leucine-rich repeat kinase 2 (LRRK2) are responsible for late-onset autosomal dominant Parkinson's disease. LRRK2 has been implicated in a wide range of physiological processes including membrane repair in the endolysosomal system. Here, using cell-free systems, we report that purified LRRK2 directly binds acidic lipid bilayers with a preference for highly curved bilayers. While this binding is nucleotide independent, LRRK2 can also deform low-curvature liposomes into narrow tubules in a guanylnucleotide-dependent but Adenosine 5'-triphosphate-independent way. Moreover, assembly of LRRK2 into scaffolds at the surface of lipid tubules can constrict them. We suggest that an interplay between the membrane remodeling and signaling properties of LRRK2 may be key to its physiological function. LRRK2, via its kinase activity, may achieve its signaling role at sites where membrane remodeling occurs.
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