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Crystal structure of the alpha appendage of AP-2 reveals a recruitment platform for clathrin-coat assembly.

AP-2 adaptors regulate clathrin-bud formation at the cell surface by recruiting clathrin trimers to the plasma membrane and by selecting certain membrane proteins for inclusion within the developing clathrin-coat structure. These functions are performed by discrete subunits of the adaptor heterotetramer. The carboxyl-terminal appendage of the AP-2 alpha subunit appears to regulate the translocation of several endocytic accessory proteins to the bud site. We have determined the crystal structure of the alpha appendage at 1.4-A resolution by multiwavelength anomalous diffraction phasing. It is composed of two distinct structural modules, a beta-sandwich domain and a mixed alpha-beta platform domain. Structure-based mutagenesis shows that alterations to the molecular surface of a highly conserved region on the platform domain differentially affect associations of the appendage with amphiphysin, eps15, epsin, and AP180, revealing a common protein-binding interface.

Pubmed ID: 10430869

Authors

  • Traub LM
  • Downs MA
  • Westrich JL
  • Fremont DH

Journal

Proceedings of the National Academy of Sciences of the United States of America

Publication Data

August 3, 1999

Associated Grants

  • Agency: NIDDK NIH HHS, Id: DK53249

Mesh Terms

  • Adaptor Proteins, Vesicular Transport
  • Amino Acid Sequence
  • Animals
  • Clathrin
  • Crystallography, X-Ray
  • Humans
  • Macromolecular Substances
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Monomeric Clathrin Assembly Proteins
  • Mutagenesis, Site-Directed
  • Nerve Tissue Proteins
  • Phosphoproteins
  • Protein Structure, Secondary
  • Recombinant Fusion Proteins