Phosphorylation of Hsl1 by Hog1 leads to a G2 arrest essential for cell survival at high osmolarity.

@article{Clotet2006PhosphorylationOH,
  title={Phosphorylation of Hsl1 by Hog1 leads to a G2 arrest essential for cell survival at high osmolarity.},
  author={J. Clotet and Xavier Escot{\'e} and Miquel Angel Mestre Adrover and Gilad Yaakov and E. Noem{\'i} Gari and Mart{\'i} Aldea and Eul{\`a}lia de Nadal and Francesc Posas},
  journal={The EMBO journal},
  year={2006},
  volume={25 11},
  pages={2338-46}
}
Control of cell cycle progression by stress-activated protein kinases (SAPKs) is essential for cell adaptation to extracellular stimuli. Exposure of yeast to osmostress leads to activation of the Hog1 SAPK, which controls cell cycle at G1 by the targeting of Sic1. Here, we show that survival to osmostress also requires regulation of G2 progression. Activated Hog1 interacts and directly phosphorylates a residue within the Hsl7-docking site of the Hsl1 checkpoint kinase, which results in… CONTINUE READING