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Gene Review

STE20  -  Ste20p

Saccharomyces cerevisiae S288c

Synonyms: Serine/threonine-protein kinase STE20, YHL007C
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Disease relevance of STE20


High impact information on STE20

  • Three alleles of BMH1 encode proteins defective for FG(TyA)-lacZ signaling and association with Ste20p, yet these alleles complement other 14-3-3 functions [3].
  • Moreover, Bmh1p and Bmh2p associate with Ste20p in vivo [3].
  • Considering the high degree of structural and functional conservation of Ste20/PAK family members and G-protein subunits, our results provide a possible model for a role of these kinases in Gbetagamma-mediated signal transduction in organisms ranging from yeast to mammals [4].
  • Serine/threonine protein kinases of the Ste20/PAK family have been implicated in the signalling from heterotrimeric G proteins to mitogen-activated protein (MAP) kinase cascades [4].
  • We have identified a binding site for the G-protein beta-subunit (Gbeta) in the non-catalytic carboxy-terminal regions of Ste20 and its mammalian homologues, the p21-activated protein kinases (PAKs) [4].

Biological context of STE20


Anatomical context of STE20

  • Lung epithelial cells and extracellular matrix components induce expression of Pneumocystis carinii STE20, a gene complementing the mating and pseudohyphal growth defects of STE20 mutant yeast [9].
  • LOK is expressed as a 130-kDa protein, which was detected predominantly in lymphoid organs such as spleen, thymus, and bone marrow, in contrast to other mammalian members of the STE20 family [10].
  • In contrast to p42MAPK, activation of JNK/SAPK in Xenopus oocyte extracts was induced by both the yeast Ste20 and Shk1 kinases, as well as by mammalian Pak1 [11].
  • Misshapen/NIKs-related kinase (MINK) is a member of the germinal center family of kinases that are homologous to the yeast sterile 20 (Ste20) kinases and regulate a wide variety of cellular processes, including cell morphology, cytoskeletal rearrangement, and survival [12].
  • PAKc contains a Rac-GTPase binding (CRIB) and autoinhibitory domain, a PAK-related kinase domain, an N-terminal phosphatidylinositol binding domain, and a C-terminal extension related to the Gbetagamma binding domain of Saccharomyces cerevisiae Ste20, the latter two domains being required for PAKc transient localization to the plasma membrane [13].

Associations of STE20 with chemical compounds


Physical interactions of STE20

  • Our genetic analyses suggest the possibility that Cdc42p and Hsl7p compete for binding to Ste20p for pseudohyphal development when starved for nitrogen [5].
  • This function of Ste20 in the HOG pathway requires binding of the small GTPase Cdc42 [17].

Enzymatic interactions of STE20

  • RESULTS: Ste20p phosphorylated Ste11p on Ser302 and/or Ser306 and Thr307 in yeast, residues that are conserved in MEKKs of other organisms [18].

Regulatory relationships of STE20

  • Thus, Hsl7p may inhibit the activity of Ste20p in the S. cerevisiae filamentous growth-signaling pathway [5].
  • We therefore propose that Akr1p negatively affects the activity of a protein that both controls cell shape and contributes to the pheromone response pathway upstream of Ste20p but downstream of G beta gamma [19].
  • Together, these results suggest that one function of Ste20p may be to activate the polarisome complex by phosphorylation of Bni1p [6].
  • Ste20 activates Ste11 by derepressing an autoinhibitory domain [20].
  • In addition, these point mutants were synthetically lethal with disruption of CLA4 and blocked the Ste20p-Cdc42p two-hybrid interaction [21].

Other interactions of STE20

  • Cla4 and Ste20 kinases apparently share a function in localizing cell growth with respect to the septin ring [7].
  • Hsl7p, a negative regulator of Ste20p protein kinase in the Saccharomyces cerevisiae filamentous growth-signaling pathway [5].
  • Thus, binding of Gbetagamma to the RING-H2 domain may induce a conformational change that promotes association of the N- and C-terminal ends of Ste5, stimulating activation of the MAPK cascade by optimizing orientation of the bound kinases and/or by increasing their accessibility to Ste20-dependent phosphorylation (or both) [22].
  • Two morphogenic pathways for which Ste20 is essential, pseudohyphal differentiation and haploid-invasive growth, also require CLN1 and CLN2 [8].
  • This effect was also seen when similarly truncated versions of Ste20p or Cla4p were overexpressed [23].

Analytical, diagnostic and therapeutic context of STE20


  1. A dominant truncation allele identifies a gene, STE20, that encodes a putative protein kinase necessary for mating in Saccharomyces cerevisiae. Ramer, S.W., Davis, R.W. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  2. Activation of Ste20 by Nef from human immunodeficiency virus induces cytoskeletal rearrangements and downstream effector functions in Saccharomyces cerevisiae. Plemenitas, A., Lu, X., Geyer, M., Veranic, P., Simon, M.N., Peterlin, B.M. Virology (1999) [Pubmed]
  3. 14-3-3 proteins are essential for RAS/MAPK cascade signaling during pseudohyphal development in S. cerevisiae. Roberts, R.L., Mösch, H.U., Fink, G.R. Cell (1997) [Pubmed]
  4. Interaction of a G-protein beta-subunit with a conserved sequence in Ste20/PAK family protein kinases. Leeuw, T., Wu, C., Schrag, J.D., Whiteway, M., Thomas, D.Y., Leberer, E. Nature (1998) [Pubmed]
  5. Hsl7p, a negative regulator of Ste20p protein kinase in the Saccharomyces cerevisiae filamentous growth-signaling pathway. Fujita, A., Tonouchi, A., Hiroko, T., Inose, F., Nagashima, T., Satoh, R., Tanaka, S. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  6. Synthetic lethal analysis implicates Ste20p, a p21-activated potein kinase, in polarisome activation. Goehring, A.S., Mitchell, D.A., Tong, A.H., Keniry, M.E., Boone, C., Sprague, G.F. Mol. Biol. Cell (2003) [Pubmed]
  7. Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast. Cvrcková, F., De Virgilio, C., Manser, E., Pringle, J.R., Nasmyth, K. Genes Dev. (1995) [Pubmed]
  8. Potential regulation of Ste20 function by the Cln1-Cdc28 and Cln2-Cdc28 cyclin-dependent protein kinases. Oehlen, L.J., Cross, F.R. J. Biol. Chem. (1998) [Pubmed]
  9. Lung epithelial cells and extracellular matrix components induce expression of Pneumocystis carinii STE20, a gene complementing the mating and pseudohyphal growth defects of STE20 mutant yeast. Kottom, T.J., Köhler, J.R., Thomas, C.F., Fink, G.R., Limper, A.H. Infect. Immun. (2003) [Pubmed]
  10. LOK is a novel mouse STE20-like protein kinase that is expressed predominantly in lymphocytes. Kuramochi, S., Moriguchi, T., Kuida, K., Endo, J., Semba, K., Nishida, E., Karasuyama, H. J. Biol. Chem. (1997) [Pubmed]
  11. Activation of mitogen-activated protein kinase cascades by p21-activated protein kinases in cell-free extracts of Xenopus oocytes. Polverino, A., Frost, J., Yang, P., Hutchison, M., Neiman, A.M., Cobb, M.H., Marcus, S. J. Biol. Chem. (1995) [Pubmed]
  12. Identification and functional characterization of a novel human misshapen/Nck interacting kinase-related kinase, hMINK beta. Hu, Y., Leo, C., Yu, S., Huang, B.C., Wang, H., Shen, M., Luo, Y., Daniel-Issakani, S., Payan, D.G., Xu, X. J. Biol. Chem. (2004) [Pubmed]
  13. Dictyostelium PAKc is required for proper chemotaxis. Lee, S., Rivero, F., Park, K.C., Huang, E., Funamoto, S., Firtel, R.A. Mol. Biol. Cell (2004) [Pubmed]
  14. Arabidopsis thaliana cDNA isolated by functional complementation shows homology to serine/threonine protein kinases. Covic, L., Lew, R.R. Biochim. Biophys. Acta (1996) [Pubmed]
  15. Differential expression of a novel protein kinase in human B lymphocytes. Preferential localization in the germinal center. Katz, P., Whalen, G., Kehrl, J.H. J. Biol. Chem. (1994) [Pubmed]
  16. Nck-interacting Ste20 kinase couples Eph receptors to c-Jun N-terminal kinase and integrin activation. Becker, E., Huynh-Do, U., Holland, S., Pawson, T., Daniel, T.O., Skolnik, E.Y. Mol. Cell. Biol. (2000) [Pubmed]
  17. Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAPK pathway. Raitt, D.C., Posas, F., Saito, H. EMBO J. (2000) [Pubmed]
  18. 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]
  19. AKR1 encodes a candidate effector of the G beta gamma complex in the Saccharomyces cerevisiae pheromone response pathway and contributes to control of both cell shape and signal transduction. Pryciak, P.M., Hartwell, L.H. Mol. Cell. Biol. (1996) [Pubmed]
  20. Pheromone response, mating and cell biology. Elion, E.A. Curr. Opin. Microbiol. (2000) [Pubmed]
  21. Genetic analysis of the interface between Cdc42p and the CRIB domain of Ste20p in Saccharomyces cerevisiae. Ash, J., Wu, C., Larocque, R., Jamal, M., Stevens, W., Osborne, M., Thomas, D.Y., Whiteway, M. Genetics (2003) [Pubmed]
  22. Mutational analysis suggests that activation of the yeast pheromone response mitogen-activated protein kinase pathway involves conformational changes in the Ste5 scaffold protein. Sette, C., Inouye, C.J., Stroschein, S.L., Iaquinta, P.J., Thorner, J. Mol. Biol. Cell (2000) [Pubmed]
  23. Characterization of SKM1, a Saccharomyces cerevisiae gene encoding a novel Ste20/PAK-like protein kinase. Martín, H., Mendoza, A., Rodríguez-Pachón, J.M., Molina, M., Nombela, C. Mol. Microbiol. (1997) [Pubmed]
  24. Fission yeast pak1+ encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating. Ottilie, S., Miller, P.J., Johnson, D.I., Creasy, C.L., Sells, M.A., Bagrodia, S., Forsburg, S.L., Chernoff, J. EMBO J. (1995) [Pubmed]
  25. Molecular cloning and characterization of a novel putative STE20-like kinase in guinea pigs. Itoh, S., Kameda, Y., Yamada, E., Tsujikawa, K., Mimura, T., Kohama, Y. Arch. Biochem. Biophys. (1997) [Pubmed]
  26. Both phosphorylation and caspase-mediated cleavage contribute to regulation of the Ste20-like protein kinase Mst1 during CD95/Fas-induced apoptosis. Graves, J.D., Draves, K.E., Gotoh, Y., Krebs, E.G., Clark, E.A. J. Biol. Chem. (2001) [Pubmed]
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