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Clathrin coat construction in endocytosis.
B M Pearse1, C J Smith, D J Owen
1Medical Research Council Laboratory of Molecular Biology, Cambridge, CB2 2QH, UK. bulbeck@mrc-lmb.cam.acuk
Current Opinion in Structural Biology
|April 8, 2000
Summary
Structural studies reveal the clathrin molecule and its assembly into a cage. New domain structures of endocytic machinery components, like the AP2 adaptor complex, clarify clathrin coat assembly events.
Area of Science:
- Cellular biology
- Structural biology
Background:
- Clathrin-mediated endocytosis is a fundamental cellular process.
- The clathrin coat, a protein lattice, drives vesicle formation.
- Understanding coat assembly dynamics is crucial for cellular function.
Purpose of the Study:
- To detail the structure of the clathrin molecule and its assembled cage.
- To elucidate the sequence of molecular recognition events in clathrin coat assembly.
Main Methods:
- Electron cryomicroscopy (cryo-EM) of the clathrin coat.
- X-ray crystallography of clathrin heavy chain domains.
- Analysis of domain structures of endocytic machinery components, including the mu2 subunit and AP2 adaptor complex alpha-appendage domain.
Main Results:
- Detailed structural information of the assembled clathrin cage.
- Insights into the domain structures of key endocytic proteins.
- Identification of critical recognition events in coat assembly.
Conclusions:
- Integrated structural data provides a comprehensive view of the clathrin molecule and its assembly.
- Newly resolved domain structures illuminate the dynamic process of clathrin coat formation and function.