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.
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
Proc. Natl. Acad. Sci. U.S.A.
Date: Aug. 03, 1999
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