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Gene Review

SLN1  -  Sln1p

Saccharomyces cerevisiae S288c

Synonyms: Osmolarity two-component system protein SLN1, Osmosensing histidine protein kinase SLN1, Tyrosine phosphatase-dependent protein 2, YIL147C, YPD2
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Disease relevance of SLN1

  • The C-terminal response regulator domains of SLN1 and SSK1 and full-length YPD1 have been overexpressed and purified from E. coli [1].

High impact information on SLN1

  • Ypd1p binds to both Sln1p and Ssk1p and mediates the multistep phosphotransfer reaction (phosphorelay) [2].
  • The transmembrane protein Sln1p contains an extracellular sensor domain and cytoplasmic histidine kinase and receiver domains, whereas the cytoplasmic protein Ssk1p contains a receiver domain [2].
  • Pbs2p was activated by MAP kinase kinase kinases (MAPKKKs) Ssk2p and Ssk22p that are under the control of the SLN1-SSK1 two-component osmosensor [3].
  • The finding of SLN1 demonstrates that a mode of signal transduction similar to the bacterial two-component design operates in eukaryotes as well [4].
  • A missense mutation in SLN1 is lethal in the absence but not in the presence of the N-end rule pathway, a ubiquitin-dependent proteolytic system [4].

Biological context of SLN1

  • SLN1 also activates an MCM1-dependent reporter gene, P-lacZ, but this function is independent of Ssk1p [5].
  • Carbon source regulation of PIS1 gene expression in Saccharomyces cerevisiae involves the MCM1 gene and the two-component regulatory gene, SLN1 [6].
  • Activated alleles of SLN1 (sln1*) were previously identified that appear to increase the level of phosphorylation of downstream targets Ssk1p and Skn7p [7].
  • In principle, the phenotype of sln1* alleles could arise from an increase in autophosphorylation or phosphotransfer activities or a decrease in an intrinsic or extrinsic dephosphorylation activity [7].
  • The multifunctional Skn7 protein is important in oxidative as well as osmotic stress; however, the Skn7p receiver domain aspartate that is the phosphoacceptor in the SLN1 pathway is dispensable for oxidative stress [8].

Anatomical context of SLN1


Associations of SLN1 with chemical compounds


Enzymatic interactions of SLN1

  • The relationship between the two Sln1p branches is unclear, however, the requirement for unphosphorylated pathway intermediates in Hog1p pathway activation and for phosphorylated intermediates in the activation of the Mcm1p reporter suggests that the two Sln1p branches are reciprocally regulated [14].

Regulatory relationships of SLN1

  • Modulation of Sln1 kinase activity in response to changes in the osmotic environment regulates the activity of the osmotic response mitogen-activated protein kinase pathway and the activity of the Skn7p transcription factor, both important for adaptation to changing osmotic stress conditions [15].
  • Phosphorylation of Sln1p inhibits the HOG1 MAP kinase osmosensing pathway via a phosphorelay mechanism including Ypd1p and the response regulator, Ssk1p [5].

Other interactions of SLN1

  • This phosphate is then sequentially transferred to Sln1p-Asp-1144, then to Ypd1p-His64, and finally to Ssk1p-Asp554 [2].
  • In contrast, we show that Sln1p activation of Skn7p requires phosphorylation of D427 [5].
  • This is the first example in yeast of a complete circuit linking a stimulus (carbon source) to gene regulation (PIS1) using a two-component regulator (SLN1) [6].
  • Two Saccharomyces cerevisiae plasma membrane-spanning proteins, Sho1 and Sln1, function during increased osmolarity to activate a mitogen-activated protein (MAP) kinase cascade [16].
  • Moreover, Hog1p activation occurred specifically through the Sln1 branch [17].

Analytical, diagnostic and therapeutic context of SLN1


  1. Differential stabilities of phosphorylated response regulator domains reflect functional roles of the yeast osmoregulatory SLN1 and SSK1 proteins. Janiak-Spens, F., Sparling, J.M., Gurfinkel, M., West, A.H. J. Bacteriol. (1999) [Pubmed]
  2. Yeast HOG1 MAP kinase cascade is regulated by a multistep phosphorelay mechanism in the SLN1-YPD1-SSK1 "two-component" osmosensor. Posas, F., Wurgler-Murphy, S.M., Maeda, T., Witten, E.A., Thai, T.C., Saito, H. Cell (1996) [Pubmed]
  3. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Maeda, T., Takekawa, M., Saito, H. Science (1995) [Pubmed]
  4. A yeast protein similar to bacterial two-component regulators. Ota, I.M., Varshavsky, A. Science (1993) [Pubmed]
  5. The yeast histidine protein kinase, Sln1p, mediates phosphotransfer to two response regulators, Ssk1p and Skn7p. Li, S., Ault, A., Malone, C.L., Raitt, D., Dean, S., Johnston, L.H., Deschenes, R.J., Fassler, J.S. EMBO J. (1998) [Pubmed]
  6. Carbon source regulation of PIS1 gene expression in Saccharomyces cerevisiae involves the MCM1 gene and the two-component regulatory gene, SLN1. Anderson, M.S., Lopes, J.M. J. Biol. Chem. (1996) [Pubmed]
  7. Altered phosphotransfer in an activated mutant of the Saccharomyces cerevisiae two-component osmosensor Sln1p. Ault, A.D., Fassler, J.S., Deschenes, R.J. Eukaryotic Cell (2002) [Pubmed]
  8. The eukaryotic two-component histidine kinase Sln1p regulates OCH1 via the transcription factor, Skn7p. Li, S., Dean, S., Li, Z., Horecka, J., Deschenes, R.J., Fassler, J.S. Mol. Biol. Cell (2002) [Pubmed]
  9. Yeast osmosensor Sln1 and plant cytokinin receptor Cre1 respond to changes in turgor pressure. Reiser, V., Raitt, D.C., Saito, H. J. Cell Biol. (2003) [Pubmed]
  10. Activation of the HOG Pathway upon Cold Stress in Saccharomyces cerevisiae. Hayashi, M., Maeda, T. J. Biochem. (2006) [Pubmed]
  11. Effects of iprodione and fludioxonil on glycerol synthesis and hyphal development in Candida albicans. Ochiai, N., Fujimura, M., Oshima, M., Motoyama, T., Ichiishi, A., Yamada-Okabe, H., Yamaguchi, I. Biosci. Biotechnol. Biochem. (2002) [Pubmed]
  12. Antifungal properties and target evaluation of three putative bacterial histidine kinase inhibitors. Deschenes, R.J., Lin, H., Ault, A.D., Fassler, J.S. Antimicrob. Agents Chemother. (1999) [Pubmed]
  13. Modulation of yeast Sln1 kinase activity by the CCW12 cell wall protein. Shankarnarayan, S., Narang, S.S., Malone, C.L., Deschenes, R.J., Fassler, J.S. J. Biol. Chem. (2008) [Pubmed]
  14. Intracellular glycerol levels modulate the activity of Sln1p, a Saccharomyces cerevisiae two-component regulator. Tao, W., Deschenes, R.J., Fassler, J.S. J. Biol. Chem. (1999) [Pubmed]
  15. Role for the Ran binding protein, Mog1p, in Saccharomyces cerevisiae SLN1-SKN7 signal transduction. Lu, J.M., Deschenes, R.J., Fassler, J.S. Eukaryotic Cell (2004) [Pubmed]
  16. A third osmosensing branch in Saccharomyces cerevisiae requires the Msb2 protein and functions in parallel with the Sho1 branch. O'Rourke, S.M., Herskowitz, I. Mol. Cell. Biol. (2002) [Pubmed]
  17. A downshift in temperature activates the high osmolarity glycerol (HOG) pathway, which determines freeze tolerance in Saccharomyces cerevisiae. Panadero, J., Pallotti, C., Rodríguez-Vargas, S., Randez-Gil, F., Prieto, J.A. J. Biol. Chem. (2006) [Pubmed]
  18. Phosphorelay-regulated degradation of the yeast Ssk1p response regulator by the ubiquitin-proteasome system. Sato, N., Kawahara, H., Toh-e, A., Maeda, T. Mol. Cell. Biol. (2003) [Pubmed]
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