FCHo Proteins Are Nucleators of Clathrin-Mediated Endocytosis
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Initiator for Coated Pit Assembly: During clathrin-mediated endocytosis, it has been thought that the sensing and binding of the clathrin adaptor protein AP2 to cargo and lipids leads to the recruitment of clathrin, nucleating the formation of a clathrin-coated pit. Henne et al. (p. 1281 , published online 6 May) have now found that this process of AP2 binding may not in fact represent either the first or the nucleation event of endocytosis. Instead, ubiquitous proteins called FCHo1/2 (F-BAR proteins) bind to the plasma membrane and define the sites of endocytosis independently of AP2. The F-BAR protein can generate very low curvature and, at higher concentration, generates higher curvature like those required at the neck of budding vesicles. The C terminus of the protein has a mu-homology domain (with homology to the mu domain of the AP2 complex) that interacts with Eps15 and intersectin, and via these proteins recruits AP2, which further recruits clathrin. Thus, a curvature-inducing protein can act to nucleate clathrin-coated pit assembly during endocytosis.
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Scaffolds such as EPS15, clathrin, intersectins, and EPS15R interact with themselves and with clathrin adaptors to cluster coat components together.
“The scaffolds such as epidermal growth factor receptor substrate 15 (EPS15), clathrin, intersectins, and epidermal growth factor receptor substrate 15 like 1 (EPS15R) interact with themselves and with the clathrin adaptors to cluster the coat components together [43,55,56].”
From Insights of Endocytosis Signaling in Health and Disease (2023) · cites this paper as [55]
The paper’s Abstract (page unavailable) identifies eps15 and intersectin as scaffold proteins that engage the adaptor AP2; it also reports that eps15, eps15R and intersectins help cluster FCHo proteins at nascent coated pits. It does not establish that these proteins interact with themselves or that clathrin is one of the scaffolds acting in this way. The paper instead describes clathrin as a coat protein recruited later. (LLM, conf=0.87)
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References 19 · Cited by 483
Research works printed but not linked: 19
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- Authors
- Henne, W. M., Boucrot, E., Meinecke, M., Evergren, E., Vallis, Y., Mittal, R., & McMahon, H. T.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Corresponding author
- Henne, William Mike
- Boucrot, Emmanuel
- McMahon, Harvey T.
- Venue
- Science
- Published
- 2010-06-04
- Volume
- 328
- Issue
- 5983
- Pages
- 1281-1284
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2883440
- OpenAlex
- W2041848251
- Cited by
- 483
- References
- 19
- Citations by year
- 2026: 17 · 2025: 22 · 2024: 18 · 2023: 30 · 2022: 37 · 2021: 33 · 2020: 27 · 2019: 22 · 2018: 27 · 2017: 21 · 2016: 25 · 2015: 26 · 2014: 34 · 2013: 36 · 2012: 48
- FWCI
- 20.01
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Research Portal (Queen's University Belfast) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Caveolin-1 and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
- Keywords
- clathrin-mediated endocytosis, F-BAR domain, membrane bending, Eps15, intersectin, AP2 adaptor complex, synaptic vesicle recycling, ligand internalization
- MeSH terms
- Animals, Calcium-Binding Proteins, Cell Line, Cell Membrane, Cells, Cultured, Clathrin, Endocytosis, HeLa Cells, Humans, Membrane Proteins, Models, Molecular, Neurons, Phosphoproteins, Proteins, Recombinant Fusion Proteins, Synaptic Vesicles, Rats, Sprague-Dawley, Protein Structure, Tertiary, Clathrin-Coated Vesicles, Adaptor Proteins, Vesicular Transport, Adaptor Protein Complex 2, RNA Interference, Intracellular Signaling Peptides and Proteins, Adaptor Proteins, Signal Transducing, Fatty Acid-Binding Proteins, Mice, Rats, Protein Multimerization
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