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http://purl.uniprot.org/citations/18211691http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18211691http://www.w3.org/2000/01/rdf-schema#comment"

Background

The appendage domain of the gammaCOP subunit of the COPI vesicle coat bears a striking structural resemblance to adaptin-family appendages despite limited primary sequence homology. Both the gammaCOP appendage domain and an equivalent region on betaCOP contain the FxxxW motif; the conservation of this motif suggested the existence of a functional appendage domain in betaCOP.

Results

Sequence comparisons in combination with structural prediction tools show that the fold of the COOH-terminus of Sec26p is strongly predicted to closely mimic that of adaptin-family appendages. Deletion of the appendage domain of Sec26p results in inviability in yeast, over-expression of the deletion construct is dominant negative and mutagenesis of this region identifies residues critical for function. The ArfGAP Glo3p was identified via suppression screening as a potential downstream modulator of Sec26p in a manner that is independent of the GAP activity of Glo3p but requires the presence of the COOH-terminal ISS motifs.

Conclusion

Together, these results indicate an essential function for the predicted betaCOP appendage and suggest that both COPI appendages perform a biologically active regulatory role with a structure related to adaptin-family appendage domains."xsd:string
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http://purl.uniprot.org/citations/18211691http://purl.uniprot.org/core/author"Cerione R.A."xsd:string
http://purl.uniprot.org/citations/18211691http://purl.uniprot.org/core/author"Collins R.N."xsd:string
http://purl.uniprot.org/citations/18211691http://purl.uniprot.org/core/author"Rahl P.B."xsd:string
http://purl.uniprot.org/citations/18211691http://purl.uniprot.org/core/author"Hoffman G.R."xsd:string
http://purl.uniprot.org/citations/18211691http://purl.uniprot.org/core/author"DeRegis C.J."xsd:string
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http://purl.uniprot.org/citations/18211691http://purl.uniprot.org/core/title"Mutational analysis of betaCOP (Sec26p) identifies an appendage domain critical for function."xsd:string
http://purl.uniprot.org/citations/18211691http://purl.uniprot.org/core/volume"9"xsd:string
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