Rules for the recognition of dilysine retrieval motifs by coatomer Journal Article


Authors: Ma, W.; Goldberg, J.
Article Title: Rules for the recognition of dilysine retrieval motifs by coatomer
Abstract: Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α-COP and β′-COP subunits and packaged into COPI-coated vesicles for Golgi-to-ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of α-COP and β′-COP bound to a series of naturally occurring retrieval motifs - encompassing KKxx, KxKxx and non-canonical RKxx and viral KxHxx sequences. Binding experiments show that α-COP and β′-COP have generally the same specificity for KKxx and KxKxx, but only β′-COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side-chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C-terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non-lysine residues. © 2013 European Molecular Biology Organization.
Keywords: vesicular transport; coatomer; copi; dilysine signal
Journal Title: EMBO Journal
Volume: 32
Issue: 7
ISSN: 0261-4189
Publisher: Wiley Blackwell  
Date Published: 2013-04-03
Start Page: 926
End Page: 937
Language: English
PROVIDER: scopus
PMCID: PMC3616288
PUBMED: 23481256
DOI: 10.1038/emboj.2013.41
DOI/URL:
Notes: --- - Cited By (since 1996):1 - "Export Date: 1 May 2013" - "CODEN: EMJOD" - ":doi 10.1038/emboj.2013.41" - "Source: Scopus"
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  1. Wenfu Ma
    4 Ma