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Gene Review

SSK1  -  mitogen-activated protein kinase kinase...

Saccharomyces cerevisiae S288c

Synonyms: Osmolarity two-component system protein SSK1, YLR006C
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Disease relevance of SSK1


High impact information on SSK1

  • Pbs2p was activated by MAP kinase kinase kinases (MAPKKKs) Ssk2p and Ssk22p that are under the control of the SLN1-SSK1 two-component osmosensor [2].
  • The SSK1 C-terminal receiver domain interacts with an N-terminal segment of SSK2 [3].
  • The histidine-containing phosphotransfer (HPt) protein YPD1 is an osmoregulatory protein in yeast that facilitates phosphoryl transfer between the two response regulator domains associated with SLN1 and SSK1 [4].
  • AhSSK1, despite having a similar secondary structure to other SKP1-like proteins, appeared quite distinctive in sequence and unique in a phylogenetic analysis, in which no SSK1 ortholog could be predicted in the sequenced genomes of Arabidopsis and rice [5].
  • Defective hyphal development and avirulence caused by a deletion of the SSK1 response regulator gene in Candida albicans [6].

Biological context of SSK1

  • Because the phosphorylation state largely determines the functional state of response regulator proteins, we have carried out a comparative study of the phosphorylated lifetimes of the three response regulator domains associated with SLN1, SSK1, and SKN7 (R1, R2, and R3, respectively) [7].
  • The results confirmed our previous observation that CaSSK1, unlike SSK1 or mcs4(+), does not regulate cellular responses to either osmotic or oxidative stress [6].
  • Finally, virulence studies indicated that SSK1 is essential for the pathogenesis of C. albicans, suggesting that the Ssk1p response regulator could be a good target for antifungal therapy [6].
  • The homologous regulatory domains of SLN1 and SSK1 exhibit remarkably different phosphorylated half-lives, a finding that provides insight into the distinct roles that these phosphorylation-dependent regulatory domains play in the yeast osmosensory signal transduction pathway [1].

Anatomical context of SSK1

  • Further, SSK1 appears to have a regulatory function in some aspects of cell wall biosynthesis [8].

Associations of SSK1 with chemical compounds

  • We have previously shown that C. albicans SSK1 does not complement the ssk1 mutant of S. cerevisiae and that the ssk1 mutant of C. albicans is not sensitive to sorbitol [8].

Other interactions of SSK1

  • Activation of the yeast SSK2 MAP kinase kinase kinase by the SSK1 two-component response regulator [3].


  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. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Maeda, T., Takekawa, M., Saito, H. Science (1995) [Pubmed]
  3. Activation of the yeast SSK2 MAP kinase kinase kinase by the SSK1 two-component response regulator. Posas, F., Saito, H. EMBO J. (1998) [Pubmed]
  4. Functional roles of conserved amino acid residues surrounding the phosphorylatable histidine of the yeast phosphorelay protein YPD1. Janiak-Spens, F., West, A.H. Mol. Microbiol. (2000) [Pubmed]
  5. AhSSK1, a novel SKP1-like protein that interacts with the S-locus F-box protein SLF. Huang, J., Zhao, L., Yang, Q., Xue, Y. Plant J. (2006) [Pubmed]
  6. Defective hyphal development and avirulence caused by a deletion of the SSK1 response regulator gene in Candida albicans. Calera, J.A., Zhao, X.J., Calderone, R. Infect. Immun. (2000) [Pubmed]
  7. Novel role for an HPt domain in stabilizing the phosphorylated state of a response regulator domain. Janiak-Spens, F., Sparling, D.P., West, A.H. J. Bacteriol. (2000) [Pubmed]
  8. Candida albicans response regulator gene SSK1 regulates a subset of genes whose functions are associated with cell wall biosynthesis and adaptation to oxidative stress. Chauhan, N., Inglis, D., Roman, E., Pla, J., Li, D., Calera, J.A., Calderone, R. Eukaryotic Cell (2003) [Pubmed]
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