ArticleBMC cell biology2008
Mutational analysis of betaCOP (Sec26p) identifies an appendage domain critical for function.
Article in BMC cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed.
- Phenotype to genotype inCurrent research in microbial sciences · 2022Article
- A Library ofFrontiers in bioengineering and biotechnology · 2021Article
- Dissection of GTPase-activating proteins reveals functional asymmetry in the COPI coat of budding yeast.Journal of cell science · 2019Article
- 9Å structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments.eLife · 2017Article
- Phosphorylation provides a negative mode of regulation for the yeast Rab GTPase Sec4p.PloS one · 2011Article
- ARFGAP2 and ARFGAP3 are essential for COPI coat assembly on the Golgi membrane of living cells.The Journal of biological chemistry · 2010Article
- Coat-tether interaction in Golgi organization.Molecular biology of the cell · 2008Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
backgroundThe 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.
resultsSequence 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.
conclusionTogether, 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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