ArticlePloS one2011
The ankyrin repeats and DHHC S-acyl transferase domain of AKR1 act independently to regulate switching from vegetative to mating states in yeast.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- A key role for sex chromosomes in the regulation of parthenogenesis in the brown alga Ectocarpus.PLoS genetics · 2019Article
- Protein palmitoylation: Palmitoyltransferases and their specificity.Experimental biology and medicine (Maywood, N.J.) · 2017Article
- Progress toward Understanding Protein S-acylation: Prospective in Plants.Frontiers in plant science · 2017Review
- Palmitoylation of the Cysteine Residue in the DHHC Motif of a Palmitoyl Transferase Mediates Ca2+ Homeostasis in Aspergillus.PLoS genetics · 2016Article
- Protein S-Acyltransferase 14: A Specific Role for Palmitoylation in Leaf Senescence in Arabidopsis.Plant physiology · 2016Article
- The Cysteine-rich Domain of the DHHC3 Palmitoyltransferase Is Palmitoylated and Contains Tightly Bound Zinc.The Journal of biological chemistry · 2015Article
- The canonical DHHC motif is not absolutely required for the activity of the yeast S-acyltransferases Swf1 and Pfa4.The Journal of biological chemistry · 2015Article
- Identification of a Novel Sequence Motif Recognized by the Ankyrin Repeat Domain of zDHHC17/13 S-Acyltransferases.The Journal of biological chemistry · 2015Article
- Polyketide synthesis genes associated with toxin production in two species of Gambierdiscus (Dinophyceae).BMC genomics · 2015Article
- The physiology of protein S-acylation.Physiological reviews · 2015Review
- Article
- Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S-acyltransferase protein family.Plant physiology · 2012Article
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2 authors.
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Abstract
Signal transduction from G-protein coupled receptors to MAPK cascades through heterotrimeric G-proteins has been described for many eukaryotic systems. One of the best-characterised examples is the yeast pheromone response pathway, which is negatively regulated by AKR1. AKR1-like proteins are present in all eukaryotes and contain a DHHC domain and six ankyrin repeats. Whilst the DHHC domain dependant S-acyl transferase (palmitoyl transferase) function of AKR1 is well documented it is not known whether the ankyrin repeats are also required for this activity. Here we show that the ankyrin repeats of AKR1 are required for full suppression of the yeast pheromone response pathway, by sequestration of the Gβγ dimer, and act independently of AKR1 S-acylation function. Importantly, the functions provided by the AKR1 ankyrin repeats and DHHC domain are not required on the same molecule to fully restore WT phenotypes and function. We also show that AKR1 molecules are S-acylated at locations other than the DHHC cysteine, increasing the abundance of AKR1 in the cell. Our results have important consequences for studies of AKR1 function, including recent attempts to characterise S-acylation enzymology and kinetics. Proteins similar to AKR1 are found in all eukaryotes and our results have broad implications for future work on these proteins and the control of switching between Gβγ regulated pathways.
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