ArticleNature communications2023
Self-assembly of CIP4 drives actin-mediated asymmetric pit-closing in clathrin-mediated endocytosis.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- In situ mapping of late-stage biomechanical coordination during clathrin-mediated endocytosis.Nature communications · 2026Article
- Efficient cellular transformation via protein delivery through the protrusion-derived extracellular vesicles.Nature communications · 2025Article
- Enhanced visualization of influenza A virus entry into living cells using virus-view atomic force microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Apical clathrin-coated pits control the location, timing, and scale of microvillar growth.Cell reports · 2025Article
- Liquid-like condensates that bind actin promote assembly and bundling of actin filaments.Developmental cell · 2025Article
- Claudin-11 plays a pivotal role in the clathrin-mediated endocytosis of influenza A virus.Science China. Life sciences · 2025Article
- Liquid-like condensates that bind actin drive filament polymerization and bundling.bioRxiv : the preprint server for biology · 2024Article
- Protein-membrane interactions: sensing and generating curvature.Trends in biochemical sciences · 2024Review
- GLT-1a glutamate transporter nanocluster localization is associated with astrocytic actin and neuronal Kv2 clusters at sites of neuron-astrocyte contact.Frontiers in cell and developmental biology · 2024Article
- A CIE change in our understanding of endocytic mechanisms.Frontiers in cell and developmental biology · 2023Review
- Cell lipid biology in infections: an overview.Frontiers in cellular and infection microbiology · 2023Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clathrin-mediated endocytosis is pivotal to signal transduction pathways between the extracellular environment and the intracellular space. Evidence from live-cell imaging and super-resolution microscopy of mammalian cells suggests an asymmetric distribution of actin fibres near the clathrin-coated pit, which induces asymmetric pit-closing rather than radial constriction. However, detailed molecular mechanisms of this 'asymmetricity' remain elusive. Herein, we used high-speed atomic force microscopy to demonstrate that CIP4, a multi-domain protein with a classic F-BAR domain and intrinsically disordered regions, is necessary for asymmetric pit-closing. Strong self-assembly of CIP4 via intrinsically disordered regions, together with stereospecific interactions with the curved membrane and actin-regulating proteins, generates a small actin-rich environment near the pit, which deforms the membrane and closes the pit. Our results provide mechanistic insights into how disordered and structured domain collaboration promotes spatio-temporal actin polymerisation near the plasma membrane.
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