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Gene Review

STE11  -  Ste11p

Saccharomyces cerevisiae S288c

Synonyms: L8039.10, Serine/threonine-protein kinase STE11, YLR362W
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Disease relevance of STE11


High impact information on STE11

  • Set2 functioned upstream of Rpd3S and the Eaf3 methyl-histone binding chromodomain was important for recruitment of Rpd3S and for deacetylation within the STE11 ORF [2].
  • Ste5 copurifies with Ste11, Fus3, and a hypophosphorylated form of Ste7, and all four proteins cosediment in a glycerol gradient as if in a large complex [3].
  • FUS3/KSS1 phosphorylation depends on two additional kinases, STE11 and STE7 (refs 2, 5, 6) [4].
  • Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold role of Pbs2p MAPKK [5].
  • Adaptor protein Ste50p links the Ste11p MEKK to the HOG pathway through plasma membrane association [6].

Biological context of STE11


Anatomical context of STE11

  • The RA domain of Ste50 adaptor protein is required for delivery of Ste11 to the plasma membrane in the filamentous growth signaling pathway of the yeast Saccharomyces cerevisiae [9].
  • Injection of recombinant STE11 protein (a yeast MAPKK kinase) also induced initiation of oocyte maturation [11].
  • Injection of an N-terminal truncated STE11 protein (delta N-STE11), a constitutively active form of STE11 which is a yeast MAPKK kinase, induced neurite outgrowth in PC12 cells [12].
  • Once Ste11 is activated, signaling through the mating pathway remains minimal but is substantially amplified when Ste5 is recruited to the membrane either by the Gbetagamma dimer or by direct membrane targeting, even to internal membranes [13].
  • Functional analysis of a C. glabrata ste11 null mutant demonstrates that Ste11 is required for adaptation to hypertonic stress but is largely dispensable for maintenance of cell wall integrity [14].

Associations of STE11 with chemical compounds

  • Requirement of STE50 for osmostress-induced activation of the STE11 mitogen-activated protein kinase kinase kinase in the high-osmolarity glycerol response pathway [15].
  • These results suggest that the Arabidopsis cDNA encodes a putative serine/threonine kinase that can function in the mating response pathway upstream of FUS3/KSS1 in S. cerevisiae, at the level of STE11 gene [16].
  • Furthermore, in the presence of cycloheximide, the STE11-induced activation of MPF as well as the induction and accumulation of Mos was blocked, and the activation of MAPK was greatly reduced [11].
  • MEK, in turn, may be activated following its phosphorylation on serine by either of the kinases encoded by proto-oncogenes raf1 or mos, as well as by p78mekk, which is related to the yeast STE11 and byr2 gene products [17].
  • Mutational analysis suggests that the leucine-rich domain limits the accessibility of the RING-H2 domain and inhibits export and recruitment in addition to promoting Ste11 association and activation [18].

Physical interactions of STE11

  • In a two-hybrid assay Ste50p interacts weakly with the G protein and strongly with the MAPKKK Ste11p [19].
  • Measurement of relative binding affinities showed that the STE11 protein tightly interacts with the STE5 protein for its stabilization [20].
  • Bud6p interacts with Ste11p [21].
  • We have found a region in the C terminus of Sho1 that binds Ste11 independently of Pbs2 and is required for crosstalk [22].
  • CDC37 overexpression also restored stable Hsp90 binding to the Ste11 protein kinase domain in the sti1Delta mutant strain [23].

Enzymatic interactions of STE11

  • RESULTS: Ste20p phosphorylated Ste11p on Ser302 and/or Ser306 and Thr307 in yeast, residues that are conserved in MEKKs of other organisms [24].

Regulatory relationships of STE11

  • Increased Cln2 levels repress the ability of hyperactive STE11 alleles to induce the pathway [25].
  • Overexpression of STE11 also suppresses the mating defects of ste50 mutants [26].
  • Nonetheless, previous work has shown that Ste11 can be activated even when Pbs2 is deleted, resulting in inappropriate crosstalk to the mating pathway [22].
  • Ste20 activates Ste11 by derepressing an autoinhibitory domain [27].
  • Byr1 and Ste7 are in turn regulated by the protein kinases Byr2 and Ste11 [28].

Other interactions of STE11

  • The second mechanism of HOG1 MAP kinase activation is independent of the two-component osmosensor and involves the SHO1 transmembrane protein and the STE11 MAPKKK [15].
  • We have found that L73A and L75A abrogate the Ste50p interaction with Ste11p, and we compare these data with the known interaction sites defined for other SAM domain interactions [29].
  • Therefore our results suggest that Cln2-dependent repression of the mating pathway occurs at the level of Ste11 [25].
  • Mutations that affect association with Ste7 or with Ste11 delineate discrete regions of Ste5 that are critical for each interaction [30].
  • Epistasis tests between dfg mutant alleles and dominant activated alleles of the RAS2 and STE11 genes, RAS2Val19 and STE11-4, respectively, identify putative targets for the filamentation signaling pathway [31].

Analytical, diagnostic and therapeutic context of STE11

  • We report here the molecular cloning of STE7 and STE11 genes and show that expression of these genes is not regulated transcriptionally by the MAT locus [8].
  • Immunodetection and Northern blot analyses showed that the low level of the STE5 protein in the ste11 delta mutant is not due to the level of gene expression but to that of protein stability [20].
  • To obtain a genomewide view of Ste11p target genes, their cell-type specificity, and their dependence on pheromone, we used DNA microarrays along with different genetic and environmental manipulations of fission yeast cells [32].


  1. Suppression of Escherichia coli alkB mutants by Saccharomyces cerevisiae genes. Wei, Y.F., Chen, B.J., Samson, L. J. Bacteriol. (1995) [Pubmed]
  2. Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription. Carrozza, M.J., Li, B., Florens, L., Suganuma, T., Swanson, S.K., Lee, K.K., Shia, W.J., Anderson, S., Yates, J., Washburn, M.P., Workman, J.L. Cell (2005) [Pubmed]
  3. Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae. Choi, K.Y., Satterberg, B., Lyons, D.M., Elion, E.A. Cell (1994) [Pubmed]
  4. MAP kinase-related FUS3 from S. cerevisiae is activated by STE7 in vitro. Errede, B., Gartner, A., Zhou, Z., Nasmyth, K., Ammerer, G. Nature (1993) [Pubmed]
  5. Osmotic activation of the HOG MAPK pathway via Ste11p MAPKKK: scaffold role of Pbs2p MAPKK. Posas, F., Saito, H. Science (1997) [Pubmed]
  6. Adaptor protein Ste50p links the Ste11p MEKK to the HOG pathway through plasma membrane association. Wu, C., Jansen, G., Zhang, J., Thomas, D.Y., Whiteway, M. Genes Dev. (2006) [Pubmed]
  7. Order of action of components in the yeast pheromone response pathway revealed with a dominant allele of the STE11 kinase and the multiple phosphorylation of the STE7 kinase. Cairns, B.R., Ramer, S.W., Kornberg, R.D. Genes Dev. (1992) [Pubmed]
  8. Molecular cloning and characterization of the STE7 and STE11 genes of Saccharomyces cerevisiae. Chaleff, D.T., Tatchell, K. Mol. Cell. Biol. (1985) [Pubmed]
  9. The RA domain of Ste50 adaptor protein is required for delivery of Ste11 to the plasma membrane in the filamentous growth signaling pathway of the yeast Saccharomyces cerevisiae. Truckses, D.M., Bloomekatz, J.E., Thorner, J. Mol. Cell. Biol. (2006) [Pubmed]
  10. Pheromone-induced signal transduction in Saccharomyces cerevisiae requires the sequential function of three protein kinases. Zhou, Z., Gartner, A., Cade, R., Ammerer, G., Errede, B. Mol. Cell. Biol. (1993) [Pubmed]
  11. Initiation of Xenopus oocyte maturation by activation of the mitogen-activated protein kinase cascade. Gotoh, Y., Masuyama, N., Dell, K., Shirakabe, K., Nishida, E. J. Biol. Chem. (1995) [Pubmed]
  12. Induction of neurite outgrowth by MAP kinase in PC12 cells. Fukuda, M., Gotoh, Y., Tachibana, T., Dell, K., Hattori, S., Yoneda, Y., Nishida, E. Oncogene (1995) [Pubmed]
  13. Dual role for membrane localization in yeast MAP kinase cascade activation and its contribution to signaling fidelity. Lamson, R.E., Takahashi, S., Winters, M.J., Pryciak, P.M. Curr. Biol. (2006) [Pubmed]
  14. Candida glabrata Ste11 is involved in adaptation to hypertonic stress, maintenance of wild-type levels of filamentation and plays a role in virulence. Calcagno, A.M., Bignell, E., Rogers, T.R., Jones, M.D., Mühlschlegel, F.A., Haynes, K. Med. Mycol. (2005) [Pubmed]
  15. Requirement of STE50 for osmostress-induced activation of the STE11 mitogen-activated protein kinase kinase kinase in the high-osmolarity glycerol response pathway. Posas, F., Witten, E.A., Saito, H. Mol. Cell. Biol. (1998) [Pubmed]
  16. Arabidopsis thaliana cDNA isolated by functional complementation shows homology to serine/threonine protein kinases. Covic, L., Lew, R.R. Biochim. Biophys. Acta (1996) [Pubmed]
  17. Networking with mitogen-activated protein kinases. Pelech, S.L., Charest, D.L., Mordret, G.P., Siow, Y.L., Palaty, C., Campbell, D., Charlton, L., Samiei, M., Sanghera, J.S. Mol. Cell. Biochem. (1993) [Pubmed]
  18. Nuclear export and plasma membrane recruitment of the Ste5 scaffold are coordinated with oligomerization and association with signal transduction components. Wang, Y., Elion, E.A. Mol. Biol. Cell (2003) [Pubmed]
  19. Ste50p sustains mating pheromone-induced signal transduction in the yeast Saccharomyces cerevisiae. Xu, G., Jansen, G., Thomas, D.Y., Hollenberg, C.P., Ramezani Rad, M. Mol. Microbiol. (1996) [Pubmed]
  20. Saccharomyces cerevisiae STE11 may contribute to the stabilities of a scaffold protein, STE5, in the pheromone signaling pathway. Kim, S.H., Lee, S.K., Choi, K.Y. Mol. Cells (1998) [Pubmed]
  21. Spa2p interacts with cell polarity proteins and signaling components involved in yeast cell morphogenesis. Sheu, Y.J., Santos, B., Fortin, N., Costigan, C., Snyder, M. Mol. Cell. Biol. (1998) [Pubmed]
  22. Sho1 and Pbs2 act as coscaffolds linking components in the yeast high osmolarity MAP kinase pathway. Zarrinpar, A., Bhattacharyya, R.P., Nittler, M.P., Lim, W.A. Mol. Cell (2004) [Pubmed]
  23. Sti1 and Cdc37 can stabilize Hsp90 in chaperone complexes with a protein kinase. Lee, P., Shabbir, A., Cardozo, C., Caplan, A.J. Mol. Biol. Cell (2004) [Pubmed]
  24. Phosphorylation of the MEKK Ste11p by the PAK-like kinase Ste20p is required for MAP kinase signaling in vivo. Drogen, F., O'Rourke, S.M., Stucke, V.M., Jaquenoud, M., Neiman, A.M., Peter, M. Curr. Biol. (2000) [Pubmed]
  25. Overexpression of the G1-cyclin gene CLN2 represses the mating pathway in Saccharomyces cerevisiae at the level of the MEKK Ste11. Wassmann, K., Ammerer, G. J. Biol. Chem. (1997) [Pubmed]
  26. Ste50p is involved in regulating filamentous growth in the yeast Saccharomyces cerevisiae and associates with Ste11p. Ramezani Rad, M., Jansen, G., Bühring, F., Hollenberg, C.P. Mol. Gen. Genet. (1998) [Pubmed]
  27. Pheromone response, mating and cell biology. Elion, E.A. Curr. Opin. Microbiol. (2000) [Pubmed]
  28. A divergence in the MAP kinase regulatory network defined by MEK kinase and Raf. Lange-Carter, C.A., Pleiman, C.M., Gardner, A.M., Blumer, K.J., Johnson, G.L. Science (1993) [Pubmed]
  29. Structure of the sterile alpha motif (SAM) domain of the Saccharomyces cerevisiae mitogen-activated protein kinase pathway-modulating protein STE50 and analysis of its interaction with the STE11 SAM. Grimshaw, S.J., Mott, H.R., Stott, K.M., Nielsen, P.R., Evetts, K.A., Hopkins, L.J., Nietlispach, D., Owen, D. J. Biol. Chem. (2004) [Pubmed]
  30. Mutational analysis of STE5 in the yeast Saccharomyces cerevisiae: application of a differential interaction trap assay for examining protein-protein interactions. Inouye, C., Dhillon, N., Durfee, T., Zambryski, P.C., Thorner, J. Genetics (1997) [Pubmed]
  31. Dissection of filamentous growth by transposon mutagenesis in Saccharomyces cerevisiae. Mösch, H.U., Fink, G.R. Genetics (1997) [Pubmed]
  32. Global roles of Ste11p, cell type, and pheromone in the control of gene expression during early sexual differentiation in fission yeast. Mata, J., B??hler, J. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
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