Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation.

@article{Braun2011Gid9AS,
  title={Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation.},
  author={Bernhard Braun and Thorsten Pfirrmann and Ruth Menssen and Kay Hofmann and Hartmut Scheel and Dieter H. Wolf},
  journal={FEBS letters},
  year={2011},
  volume={585 24},
  pages={3856-61}
}
The two major antagonistic pathways of carbon metabolism in cells, glycolysis and gluconeogenesis, are tightly regulated. In the eukaryotic model organism Saccharomyces cerevisiae the switch from gluconeogenesis to glycolysis is brought about by proteasomal degradation of the gluconeogenic enzyme fructose-1,6-bisphosphatase. The ubiquitin ligase responsible for polyubiquitylation of fructose-1,6-bisphosphatase is the Gid complex. This complex consists of seven subunits of which subunit Gid2… CONTINUE READING

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