ArticleThe Journal of biological chemistry2014
Dynamin1 is a novel target for IRSp53 protein and works with mammalian enabled (Mena) protein and Eps8 to regulate filopodial dynamics.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 31 citations in OpenAlex.
- Phase separation drives cortical enrichment of the F-BAR proteins Rga7 and Rga8 to maintain cell integrity.Cellular and molecular life sciences : CMLS · 2025Article
- Insulin receptor tyrosine kinase substrate in health and disease (Review).Molecular medicine reports · 2025Review
- Organization of a cytoskeletal superstructure in the apical domain of intestinal tuft cells.The Journal of cell biology · 2024Article
- Spatiotemporal coordination of actin regulators generates invasive protrusions in cell-cell fusion.Nature cell biology · 2024Article
- Molecular Relay Stations in Membrane Nanotubes: IRSp53 Involved in Actin-Based Force Generation.International journal of molecular sciences · 2023Article
- BioID2 screening identifies KIAA1671 as an EPS8 proximal factor that marks sites of microvillus growth.Molecular biology of the cell · 2023Article
- Molecular architecture of postsynaptic Interactomes.Cellular signalling · 2020Review
- IRSp53 controls plasma membrane shape and polarized transport at the nascent lumen in epithelial tubules.Nature communications · 2020Article
- Palmitoylated Proteins in Dendritic Spine Remodeling.Frontiers in synaptic neuroscience · 2020Article
- Superresolution microscopy reveals distinct localisation of full length IRSp53 and its I-BAR domain protein within filopodia.Scientific reports · 2019Article
- BAR domain proteins-a linkage between cellular membranes, signaling pathways, and the actin cytoskeleton.Biophysical reviews · 2018Review
- Deciphering the BAR code of membrane modulators.Cellular and molecular life sciences : CMLS · 2017Review
- Dynamin Autonomously Regulates Podocyte Focal Adhesion Maturation.Journal of the American Society of Nephrology : JASN · 2017Article
- Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State.Cell reports · 2017Article
- Redundant functions of I-BAR family members, IRSp53 and IRTKS, are essential for embryonic development.Scientific reports · 2017Article
- Differential identity of Filopodia and Tunneling Nanotubes revealed by the opposite functions of actin regulatory complexes.Scientific reports · 2016Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Filopodia are dynamic actin-based structures that play roles in processes such as cell migration, wound healing, and axonal guidance. Cdc42 induces filopodial formation through IRSp53, an Inverse-Bin-Amphiphysins-Rvs (I-BAR) domain protein. Previous work from a number of laboratories has shown that IRSp53 generates filopodia by coupling membrane protrusion with actin dynamics through its Src homology 3 domain binding partners. Here, we show that dynamin1 (Dyn1), the large guanosine triphosphatase, is an interacting partner of IRSp53 through pulldown and Förster resonance energy transfer analysis, and we explore its role in filopodial formation. In neuroblastoma cells, Dyn1 localizes to filopodia, associated tip complexes, and the leading edge just behind the anti-capping protein mammalian enabled (Mena). Dyn1 knockdown reduces filopodial formation, which can be rescued by overexpressing wild-type Dyn1 but not the GTPase mutant Dyn1-K44A and the loss-of-function actin binding domain mutant Dyn1-K/E. Interestingly, dynasore, an inhibitor of Dyn GTPase, also reduced filopodial number and increased their lifetime. Using rapid time-lapse total internal reflection fluorescence microscopy, we show that Dyn1 and Mena localize to filopodia only during initiation and assembly. Dyn1 actin binding domain mutant inhibits filopodial formation, suggesting a role in actin elongation. In contrast, Eps8, an actin capping protein, is seen most strongly at filopodial tips during disassembly. Taken together, the results suggest IRSp53 partners with Dyn1, Mena, and Eps8 to regulate filopodial dynamics.
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