A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex

Bernard T. Kelly, Airlie J. McCoy, Kira Späte, Sharon E. Miller, Philip R. Evans, Stefan Höning and David J. Owen ()
Additional contact information
Bernard T. Kelly: University of Cambridge, Addenbrooke’s Hospital, Hills Road, Cambridge CB2 0XY, UK
Airlie J. McCoy: University of Cambridge, Addenbrooke’s Hospital, Hills Road, Cambridge CB2 0XY, UK
Kira Späte: Institute of Biochemistry I and Center for Molecular Medicine Cologne, University of Cologne, Joseph-Stelzmann-Strasse 52, 50931 Cologne, Germany
Sharon E. Miller: University of Cambridge, Addenbrooke’s Hospital, Hills Road, Cambridge CB2 0XY, UK
Philip R. Evans: Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK
Stefan Höning: Institute of Biochemistry I and Center for Molecular Medicine Cologne, University of Cologne, Joseph-Stelzmann-Strasse 52, 50931 Cologne, Germany
David J. Owen: University of Cambridge, Addenbrooke’s Hospital, Hills Road, Cambridge CB2 0XY, UK

Nature, 2008, vol. 456, issue 7224, 976-979

Abstract: AP2 clathrin adaptor: target recognition unveiled The movement of most transmembrane proteins between the various membranes of the cell is directed by short linear amino acid sequences in their cytoplasmic portions. These sequence motifs are bound by protein components of transport vesicle coats thereby incorporating the transmembrane proteins as vesicle cargo. In the case of clathrin-coated vesicles (CCVs) the motifs are recognised by the AP complexes or GGA clathrin adaptors. The clathrin adaptor AP2 recognizes two major classes of endocytic motifs including an acidic dileucine motif. In this study, Kelly et al. present the crystal structure of AP2 in a complex with the dileucine motif of a cargo protein thereby revealing the mechanism of cargo-adaptor recognition.

Date: 2008
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/nature07422 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:456:y:2008:i:7224:d:10.1038_nature07422

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature07422

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().