Clathrin coat construction in endocytosis

Curr Opin Struct Biol. 2000 Apr;10(2):220-8. doi: 10.1016/s0959-440x(00)00071-3.

Abstract

Electron cryomicroscopy of the clathrin coat and X-ray crystallography of parts of the clathrin heavy chain combine to give a detailed picture of the clathrin molecule, assembled as a cage. Recently determined domain structures of other components of the endocytic machinery, particularly the mu2 subunit and the alpha-appendage domain of the AP2 adaptor complex, provide important information on the sequence of recognition events involved in the dynamic process of clathrin coat assembly.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adaptor Protein Complex 1*
  • Adaptor Protein Complex 2
  • Adaptor Protein Complex 3*
  • Adaptor Protein Complex alpha Subunits
  • Adaptor Protein Complex mu Subunits*
  • Adaptor Proteins, Vesicular Transport
  • Animals
  • Clathrin / chemistry*
  • Clathrin / physiology
  • Clathrin / ultrastructure
  • Coated Pits, Cell-Membrane / chemistry*
  • Cryoelectron Microscopy
  • Crystallography, X-Ray
  • Endocytosis / physiology*
  • Humans
  • Membrane Proteins / chemistry
  • Membrane Proteins / physiology
  • Models, Molecular
  • Protein Conformation

Substances

  • AP1M2 protein, human
  • AP3M2 protein, human
  • Adaptor Protein Complex 1
  • Adaptor Protein Complex 2
  • Adaptor Protein Complex 3
  • Adaptor Protein Complex alpha Subunits
  • Adaptor Protein Complex mu Subunits
  • Adaptor Proteins, Vesicular Transport
  • Clathrin
  • Membrane Proteins
  • adaptor protein complex 1, mu 2 subunit
  • adaptor protein complex 2, mu 2 subunit