ArticleDevelopmental cell2015
An organized co-assembly of clathrin adaptors is essential for endocytosis.
Article in Developmental cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 85 citations in OpenAlex.
- Clathrin adaptors drive phase separation in endocytosis and trafficking.Communications biology · 2026Article
- Competitive binding of actin and SH3 domains at proline-rich regions of Las17/WASP regulates actin polymerisation.Communications biology · 2025Article
- Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies.Nature structural & molecular biology · 2025Article
- Subtleties in Clathrin heavy chain binding boxes provide selectivity among adaptor proteins of budding yeast.Nature communications · 2024Article
- Mechanistic divergences of endocytic clathrin-coated vesicle formation in mammals, yeasts and plants.Journal of cell science · 2024Review
- Light-dependent inhibition of clathrin-mediated endocytosis in yeast unveils conserved functions of the AP2 complex.iScience · 2023Article
- Force redistribution in clathrin-mediated endocytosis revealed by coiled-coil force sensors.Science advances · 2023Article
- A Review of Mechanics-Based Mesoscopic Membrane Remodeling Methods: Capturing Both the Physics and the Chemical Diversity.The Journal of membrane biology · 2022Review
- Load adaptation by endocytic actin networks.Molecular biology of the cell · 2022Article
- Biophysical Screening Pipeline for Cryo-EM Grid Preparation of Membrane Proteins.Frontiers in molecular biosciences · 2022Article
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- Cooperative regulation of endocytic vesicle transport by yeast Eps15-like protein Pan1p and epsins.The Journal of biological chemistry · 2021Article
- Multiple roles for actin in secretory and endocytic pathways.Current biology : CB · 2021Review
- Structure of the endocytic adaptor complex reveals the basis for efficient membrane anchoring during clathrin-mediated endocytosis.Nature communications · 2021Article
- Cooperativity of membrane-protein and protein-protein interactions control membrane remodeling by epsin 1 and affects clathrin-mediated endocytosis.Cellular and molecular life sciences : CMLS · 2021Article
- Global Identification ofFrontiers in plant science · 2021Article
- The protein architecture of the endocytic coat analyzed by FRET microscopy.Molecular systems biology · 2020Article
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- Further insights from structural mass spectrometry into endocytosis adaptor protein assemblies.International journal of mass spectrometry · 2020Article
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Authors and funding
15 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Clathrin-mediated endocytosis, the main trafficking route from the plasma membrane to the cytoplasm, is critical to many fundamental cellular processes. Clathrin, coupled to the membrane by adaptor proteins, is thought to play a major structural role in endocytosis by self-assembling into a cage-like lattice around the forming vesicle. Although clathrin adaptors are essential for endocytosis, little is known about their structural role in this process. Here we show that the membrane-binding domains of two conserved clathrin adaptors, Sla2 and Ent1, co-assemble in a PI(4,5)P2-dependent manner to form organized lattices on membranes. We determined the structure of the co-assembled lattice by electron cryo-microscopy and designed mutations that specifically impair the lattice formation in vitro. We show that these mutations block endocytosis in vivo. We suggest that clathrin adaptors not only link the polymerized clathrin to the membrane but also form an oligomeric structure, which is essential for membrane remodeling during endocytosis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.