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

Authors: Traub, LM  Downs, MA  Westrich, JL  Fremont, DH 
Citation: Traub LM, etal., Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):8907-12.
Pubmed: (View Article at PubMed) PMID:10430869

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.

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CRRD Object Information
CRRD ID: 11041016
Created: 2016-03-19
Species: All species
Last Modified: 2016-03-19
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.