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Updated: May 1, 2026
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Visualizing Clathrin-mediated Endocytosis of G Protein-coupled Receptors at Single-event Resolution via TIRF Microscopy
Published on: October 20, 2014
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Membrane fluctuations destabilize clathrin protein lattice order
Nicholas Cordella1, Thomas J Lampo2, Shafigh Mehraeen3
1Chemical Engineering, Stanford University, Stanford, California; Stanford Institute for Materials and Energy Sciences, SLAC National Accelerator Laboratory, Menlo Park, California.
Biophysical Journal
|April 8, 2014
Summary
Membrane tension influences clathrin protein lattice structure. High tension stabilizes ordered crystalline lattices, while low tension results in disordered, fluidlike lattices, highlighting the role of physical cues in protein self-assembly.
Area of Science:
- Biophysics
- Cell Biology
- Materials Science
Background:
- Clathrin-mediated endocytosis involves the self-assembly of clathrin protein lattices.
- The physical properties of the cell membrane can influence protein lattice formation.
Purpose of the Study:
- To theoretically model clathrin lattice formation on a flexible membrane.
- To investigate the effect of membrane tension on clathrin lattice structure and phase behavior.
Main Methods:
- Developed a theoretical model of clathrin subunits as three-legged pinwheels with elastic properties.
- Simulated clathrin lattice behavior on an elastic sheet using Monte Carlo methods.
- Applied principles of two-dimensional melting theory.
Main Results:
- High membrane tension promotes the formation of large, flat crystalline clathrin lattices.
- Low membrane tension leads to disordered, fluidlike clathrin lattices with defects.
- Membrane tension significantly impacts the stability and order of clathrin protein assemblies.
Conclusions:
- Environmental physical cues, specifically membrane tension, are critical for dictating the collective behavior of self-assembled protein structures.
- The study provides insights into how physical forces shape cellular protein organization.
- Findings suggest a mechanism for clathrin plaque formation on adhered cell membranes.
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