The yeasts phosphorelay systems: a comparative view

  • Griselda Salas-Delgado
  • Laura Ongay-Larios
  • Laura Kawasaki-Watanabe
  • Imelda López-Villaseñor
  • Roberto Coria


Cells contain signal transduction pathways that mediate communication between the extracellular environment and the cell interior. These pathways control transcriptional programs and posttranscriptional processes that modify cell metabolism in order to maintain homeostasis. One type of these signal transduction systems are the so-called Two Component Systems (TCS), which conduct the transfer of phosphate groups between specific and conserved histidine and aspartate residues present in at least two proteins; the first protein is a sensor kinase which autophosphorylates a histidine residue in response to a stimulus, this phosphate is then transferred to an aspartic residue located in a response regulator protein. There are classical and hybrid TCS, whose difference consists in the number of proteins and functional domains involved in the phosphorelay. The TCS are widespread in bacteria where the sensor and its response regulator are mostly specific for a given stimulus. In eukaryotic organisms such as fungi, slime molds, and plants, TCS are present as hybrid multistep phosphorelays, with a variety of arrangements (Stock et al. in Annu Rev Biochem 69:183–215, 2000; Wuichet et al. in Curr Opin Microbiol 292:1039–1050, 2010). In these multistep phosphorelay systems, several phosphotransfer events take place between different histidine and aspartate residues localized in specific domains present in more than two proteins (Thomason and Kay, in J Cell Sci 113:3141–3150, 2000; Robinson et al. in Nat Struct Biol 7:626–633, 2000). This review presents a brief and succinct description of the Two-component systems of model yeasts, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Candida albicans, Cryptococcus neoformans and Kluyveromyces lactis. We have focused on the comparison of domain organization and functions of each component present in these phosphorelay systems.


Two-component systems Phosphorelay Phosphotransfer activity MAP kinase Yeast 



Partially supported by DGAPA, UNAM, PAPIIT Grant No. IN210616 and CONACyT Grant No. CB-254078. G-SD received a student fellowship from CONACyT and was a PhD student of the Biochemical Science Program while working in this topic.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.


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© Springer Science+Business Media Dordrecht 2017

Authors and Affiliations

  1. 1.Departamento de Genética Molecular, Instituto de FisiologíaCelularUniversidad Nacional Autónoma de MéxicoCiudad de MéxicoMéxico
  2. 2.Unidad de Biología Molecular, Instituto de Fisiología CelularUniversidad Nacional Autónoma de MéxicoCiudad de MéxicoMéxico
  3. 3.Departamento de Biología Molecular y Biotecnología, Instituto de Investigaciones BiomédicasUniversidad Nacional Autónoma de MéxicoCiudad de MéxicoMéxico

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