Mutational analysis of betaCOP (Sec26p) identifies an appendage domain critical for function

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 th...

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Veröffentlicht in:	BMC cell biology 2008-01, Vol.9, p.3
Hauptverfasser:	DeRegis, Carol J, Rahl, Peter B, Hoffman, Gregory R, Cerione, Richard A, Collins, Ruth N
Format:	Artikel
Sprache:	eng
Schlagworte:	Adaptor Protein Complex alpha Subunits - genetics Adaptor Protein Complex alpha Subunits - metabolism Amino Acid Motifs - genetics Base Sequence - genetics Coatomer Protein - chemistry Coatomer Protein - genetics COP-Coated Vesicles - genetics COP-Coated Vesicles - metabolism COP-Coated Vesicles - ultrastructure Endoplasmic Reticulum, Rough - metabolism Gene Expression Regulation, Fungal - genetics Golgi Apparatus - metabolism GTPase-Activating Proteins - genetics GTPase-Activating Proteins - metabolism Mutagenesis, Site-Directed Mutation - genetics Protein Structure, Tertiary - genetics Protein Transport - physiology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism
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