Phosphoproteomic analysis of protein kinase C signaling in Saccharomyces cerevisiae reveals Slt2 mitogen-activated protein kinase (MAPK)-dependent phosphorylation of eisosome core components.

@article{Mascaraque2013PhosphoproteomicAO,
  title={Phosphoproteomic analysis of protein kinase C signaling in Saccharomyces cerevisiae reveals Slt2 mitogen-activated protein kinase (MAPK)-dependent phosphorylation of eisosome core components.},
  author={Victoria Mascaraque and Mar{\'i}a Luisa Hern{\'a}ez and Mar{\'i}a Jim{\'e}nez-S{\'a}nchez and Rasmus S\ogaard Hansen and Concha Gil and Humberto Mart{\'i}n and V{\'i}ctor J Cid and Mar{\'i}a Molina},
  journal={Molecular & cellular proteomics : MCP},
  year={2013},
  volume={12 3},
  pages={557-74}
}
The cell wall integrity (CWI) pathway of the model organism Saccharomyces cerevisiae has been thoroughly studied as a paradigm of the mitogen-activated protein kinase (MAPK) pathway. It consists of a classic MAPK module comprising the Bck1 MAPK kinase kinase, two redundant MAPK kinases (Mkk1 and Mkk2), and the Slt2 MAPK. This module is activated under a variety of stimuli related to cell wall homeostasis by Pkc1, the only member of the protein kinase C family in budding yeast. Quantitative… CONTINUE READING
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