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Updated: Nov 19, 2025

A Nanobar-Supported Lipid Bilayer System for the Study of Membrane Curvature Sensing Proteins in vitro
Published on: November 30, 2022
Clathrin senses membrane curvature.
Wade F Zeno1, Jacob B Hochfelder2, Ajay S Thatte2
1Department of Biomedical Engineering, The University of Texas at Austin, Austin, Texas; Department of Chemical Engineering, The University of Southern California, Los Angeles, California.
Clathrin coat assembly, not individual proteins, senses membrane curvature. This protein network sensitivity is amplified by adaptor proteins, crucial for precise membrane remodeling in cellular processes like endocytosis.
Area of Science:
- Cell Biology
- Biophysics
- Molecular Biology
Background:
- Protein assembly at curved membranes is vital for cellular functions like endocytosis.
- Adaptor proteins recruit clathrin coats to curved membrane regions.
- It was unclear if clathrin itself senses curvature or is passively recruited.
Purpose of the Study:
- To investigate if the clathrin coat actively senses membrane curvature.
- To compare clathrin's curvature sensing ability with adaptor proteins.
- To understand the role of clathrin assembly in curvature detection.
Main Methods:
- Utilized a synthetic tag to induce clathrin assembly directly on membrane surfaces.
- Quantified clathrin's ability to sense and assemble at high membrane curvature.
- Measured the amplification of curvature sensitivity when clathrin is recruited by adaptors.
Main Results:
- Clathrin assembly, not unassembled triskelia, strongly senses membrane curvature.
- Clathrin's curvature sensitivity is comparable to known adaptor proteins.
- Adaptor-mediated recruitment amplifies clathrin's curvature sensitivity 2- to 10-fold.
Conclusions:
- Clathrin acts as a potent sensor of membrane curvature through its assembly process.
- A synergistic relationship between clathrin coat and adaptors enhances precision in membrane traffic.
- Protein networks, not individual domains, are likely key drivers of membrane curvature sensing.
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