The N-terminal half of Cdc25 is essential for processing glucose signaling in Saccharomyces cerevisiae.

@article{Gross1999TheNH,
  title={The N-terminal half of Cdc25 is essential for processing glucose signaling in Saccharomyces cerevisiae.},
  author={Avner Gross and Shira Winograd and Irit Marbach and Alexander Levitzki},
  journal={Biochemistry},
  year={1999},
  volume={38 40},
  pages={13252-62}
}
Saccharomyces cerevisiae Cdc25 is the prototype Ras GDP/GTP exchange protein. Its C-terminal catalytic domain was found to be highly conserved in the homologues p140(ras-GRF) and Sos. The regulatory domains in each Ras exchanger mediate the signals arriving from upstream elements such as tyrosine kinases for Sos, or Ca2+ and G proteins for p140.(Ras-GRF) In this study, we show that the N-terminal half (NTH) of S. cerevisiae Cdc25, as well as the C-terminal 37 amino acids, is essential for… CONTINUE READING

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