ArticleScientific reports2019
Superresolution microscopy reveals distinct localisation of full length IRSp53 and its I-BAR domain protein within filopodia.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- CCT8 associates with the MYO10 motor domain and regulates filopodia and breast cancer cell invasion.Journal of cell science · 2026Article
- Filopodial protrusion driven by density-dependent Ena-TOCA-1 interactions.Journal of cell science · 2024Article
- The cellular protrusions for inter-cellular material transfer: similarities between filopodia, cytonemes, tunneling nanotubes, viruses, and extracellular vesicles.Frontiers in cell and developmental biology · 2024Review
- Molecular Relay Stations in Membrane Nanotubes: IRSp53 Involved in Actin-Based Force Generation.International journal of molecular sciences · 2023Article
- Activated I-BAR IRSp53 clustering controls the formation of VASP-actin-based membrane protrusions.Science advances · 2022Article
- Prognostic value and immunological role of BAIAP2L2 in liver hepatocellular carcinoma: A pan-cancer analysis.Frontiers in surgery · 2022Article
- The WAVE complex associates with sites of saddle membrane curvature.The Journal of cell biology · 2021Article
- Initiation and disassembly of filopodia tip complexes containing VASP and lamellipodin.Molecular biology of the cell · 2020Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Superresolution microscopy offers the advantage of imaging biological structures within cells at the nano-scale. Here we apply two superresolution microscopy techniques, specifically 3D structured illumination microscopy (3D-SIM) and direct stochastic optical reconstruction microscopy (dSTORM), a type of single molecule localisation microscopy, to localise IRSp53 protein and its I-BAR domain in relation to F-actin within filopodia. IRSp53 generates dynamic (extending and retracting) filopodia 300 nm wide with a distinct gap between IRSp53 and F-actin. By contrast, protrusions induced by the I-BAR domain alone are non-dynamic measuring between 100-200 nm in width and exhibit a comparatively closer localisation of the I-BAR domain with the F-actin. The data suggest that IRSp53 membrane localisation is spatially segregated to the lateral edges of filopodia, in contrast to the I-BAR domain is uniformly distributed throughout the membranes of protrusions. Modeling of fluorescence recovery after photobleaching (FRAP) data suggests that a greater proportion of I-BAR domain is associated with membranes when compared to full length IRSp53. The significance of this new data relates to the role filopodia play in cell migration and its importance to cancer.
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