Clathrin.
Clathrin was discovered nearly 25 years ago. Since then, a large number of other proteins that participate in the process by which clathrin-coated vesicles retrieve synaptic membranes or take up endocytic receptors have been identified. The functional relationships among these disparate components remain, in many cases, obscure. High-resolution structures of parts of clathrin, determined by X-ray crystallography, and lower-resolution images of assembled coats, determined by electron cryomicroscopy, now provide the information necessary to integrate various lines of evidence and to design experiments that test specific mechanistic notions. This review summarizes and illustrates the recent structural results and outlines what is known about coated-vesicle assembly in the context of this information.
Kirchhausen
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Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA. Kirchhausen@crystal.harvard.edu
D000595:Amino Acid Sequence; D000818:Animals; D002966:Clathrin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D003034:Coated Pits, Cell-Membrane / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017386:Sequence Homology, Amino Acid
D002966:Clathrin