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Energetics of clathrin basket assembly
1Laboratory of Integrative and Medical Biophysics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA. rjn@helix.nih.gov
Traffic (Copenhagen, Denmark)
|March 15, 2001
Summary
This study models clathrin basket assembly using thermodynamics. Assembly energies are small, suggesting thermodynamic fluctuations drive lattice remodeling, while assembly proteins stabilize basket formation.
Area of Science:
- Biophysics
- Structural Biology
- Cell Biology
Background:
- Clathrin baskets are essential protein coats for intracellular trafficking.
- Understanding the thermodynamics of clathrin assembly is crucial for elucidating basket formation dynamics.
Purpose of the Study:
- To develop a thermodynamic model for in vitro clathrin basket assembly.
- To estimate assembly energies and the impact of assembly proteins (APs) on basket formation.
Main Methods:
- A minimal thermodynamic model incorporating bending, flexing, curvature, and interaction energies.
- Derivation of analytical expressions for basket size distributions.
- Analysis of published clathrin basket size distribution data.
Main Results:
- Estimated net total basket assembly energies are small (order of kBT).
- Thermodynamic fluctuations likely drive lattice remodeling during basket formation.
- Assembly proteins increase triskelion curvature, leg interaction stability, and effective rigidity.
Conclusions:
- Clathrin basket assembly is governed by small energy changes, allowing for dynamic remodeling.
- Assembly proteins play a significant role in stabilizing clathrin lattice formation by modulating key physical parameters.