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

BMC Cell Biology
Carol J DeRegisRuth N Collins

Abstract

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. 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. 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.

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Citations

Sep 23, 2010·The Journal of Biological Chemistry·Fredrik KartbergJohn F Presley
Apr 25, 2008·Molecular Biology of the Cell·Yusong GuoAdam D Linstedt
Jul 25, 2019·Journal of Cell Science·Eric C ArakelBlanche Schwappach

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Datasets Mentioned

BETA
AAT12307.1

Methods Mentioned

BETA
GTPase
nucleotide exchange
PCR
ISS
single knockout
restriction digest
electrophoresis

Software Mentioned

Swiss
Pdb Viewer
BLAST
CLUSTALX
DeepView
mGenTHREADER
Clustal
PSIPRED
AutoDeblur
IPLab

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