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13:28
High-resolution Single Particle Analysis from Electron Cryo-microscopy Images Using SPHIRE
Published on: May 16, 2017
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Molecular model for a complete clathrin lattice from electron cryomicroscopy
Alexander Fotin1, Yifan Cheng, Piotr Sliz
1Biophysics Graduate Program, Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Nature
|October 27, 2004
Summary
Researchers mapped the structure of clathrin lattices, revealing how these protein coats assemble. Specific interactions stabilize the lattice, controlling membrane traffic in cells.
Area of Science:
- Cell biology
- Structural biology
- Biophysics
Background:
- Clathrin-coated vesicles are essential for intracellular membrane traffic.
- Understanding clathrin lattice structure is key to deciphering its role in cellular processes.
Purpose of the Study:
- To determine the high-resolution structure of clathrin lattices.
- To elucidate the molecular interactions stabilizing the clathrin coat.
Main Methods:
- Electron cryomicroscopy (cryo-EM) of in vitro assembled clathrin coats.
- Fitting known crystal structures and homology models into the cryo-EM density map.
- Analysis of clathrin coats with varying diameters.
Main Results:
- Subnanometre resolution structure of the clathrin lattice was obtained.
- The positions of clathrin heavy and light chains were defined.
- An invariant local interaction pattern involving a helical tripod was identified, stabilizing the lattice.
Conclusions:
- The clathrin lattice is stabilized by conserved local interactions between triskelions.
- Assembly and disassembly are likely regulated by specific site events.
- This structural insight advances our understanding of membrane trafficking mechanisms.
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