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Unusual structural organization of the endocytic proteins AP180 and epsin 1.

Authors: Kalthoff, Christoph  Alves, J├╝rgen  Urbanke, Claus  Knorr, Ruth  Ungewickell, Ernst J 
Citation: Kalthoff C, etal., J Biol Chem. 2002 Mar 8;277(10):8209-16. Epub 2001 Dec 26.
Pubmed: (View Article at PubMed) PMID:11756460
DOI: Full-text: DOI:10.1074/jbc.M111587200

Epsin and AP180/CALM are important endocytic accessory proteins that are believed to be involved in the formation of clathrin coats. Both proteins associate with phosphorylated membrane inositol lipids through their epsin N-terminal homology domains and with other components of the endocytic machinery through short peptide motifs in their carboxyl-terminal segments. Using hydrodynamic and spectroscopic methods, we demonstrate that the parts of epsin 1 and AP180 that are involved in protein-protein interactions behave as poorly structured flexible polypeptide chains with little or no conventional secondary structure. The predominant cytosolic forms of both proteins are monomers. Furthermore, we show that recombinant epsin 1, like AP180, drives in vitro assembly of clathrin cages. We conclude that the epsin N-terminal homology domain-containing proteins AP180/CALM and epsin 1 have a very similar molecular architecture that is designed for the rapid and efficient recruitment of the principal coat components clathrin and AP-2 at the sites of coated pit assembly.

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CRRD Object Information
CRRD ID: 12793027
Created: 2017-03-18
Species: All species
Last Modified: 2017-03-18
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.