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The Ste20p protein kinase was immunopurified from yeast cells
and analyzed in an in vitro assay system. Ste20p immune
complexes exhibited autophosphorylating activity at serine and
threonine residues and specifically phosphorylated a bacterially
expressed glutathione S-transferase (GST) fusion of Ste11p (a
mitogen-activated protein or extracellular signal-regulated kinase
kinase (MEK) kinase homologue) at serine and threonine residues. In
contrast, GST fusions either of Ste7p (a MEK homologue) or the
Volume 270,
Number 27,
Issue of July 07, pp. 15984-15992, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
-subunit of the mating response G-protein and immunoprecipitated
Ste5p were not phosphorylated by the Ste20p immune complexes. Myelin
basic protein was identified as an excellent in vitro substrate, whereas histone H1 was only poorly phosphorylated.
Evidence was obtained that autophosphorylation might play a regulatory
role for the in vitro kinase activity. The in vitro activity was found to be Ca-independent. Both
the in vivo and in vitro activities were abolished by
mutational changes of either the conserved lysine residue 649 within
the ATP binding site or threonine 777 between the catalytic subdomains
VII and VIII. Wild-type Ste20p and the catalytically inactive T777A
mutant were identified as phosphoproteins in vivo. The
phosphorylation occurred at serine and threonine residues independent
of pheromone stimulation. Based on the genetically determined
significance of Ste20p in pheromone signal transduction and on our in vitro studies, we propose the model that Ste20p represents
a yeast MEK kinase kinase whose function is to link G-protein-coupled
receptors through G
to a mitogen-activated protein
kinase module.
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J G Cook, L Bardwell, S J Kron, and J Thorner Two novel targets of the MAP kinase Kss1 are negative regulators of invasive growth in the yeast Saccharomyces cerevisiae. Genes & Dev., November 15, 1996; 10(22): 2831 - 2848. [Abstract] [PDF]
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E. Leberer, D. Harcus, I. D. Broadbent, K. L. Clark, D. Dignard, K. Ziegelbauer, A. Schmidt, N. A. R. Gow, A. J. P. Brown, and D. Y. Thomas Signal transduction through homologs of the Ste20p and Ste7p protein kinases can trigger hyphal formation in the pathogenic fungus Candida albicans PNAS, November 12, 1996; 93(23): 13217 - 13222. [Abstract] [Full Text] [PDF]
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S.-F. Lee, T. T. Egelhoff, A. Mahasneh, and G. P. Cote Cloning and Characterization of a Dictyostelium Myosin I Heavy Chain Kinase Activated by Cdc42 and Rac J. Biol. Chem., October 25, 1996; 271(43): 27044 - 27048. [Abstract] [Full Text] [PDF]
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J. M. Kyriakis and J. Avruch Sounding the Alarm: Protein Kinase Cascades Activated by Stress and Inflammation J. Biol. Chem., October 4, 1996; 271(40): 24313 - 24316. [Full Text] [PDF]
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 T. Leeuw, A. Fourest-Lieuvin, C. Wu, J. Chenevert, K. Clark, M. Whiteway, D. Y. Thomas, and E. Leberer Pheromone Response in Yeast: Association of Bem1p with Proteins of the MAP Kinase Cascade and Actin Science, November 17, 1995; 270(5239): 1210 - 1213. [Abstract] [PDF]
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M. Whiteway, C Wu, T Leeuw, K Clark, A Fourest-Lieuvin, D. Thomas, and E Leberer Association of the yeast pheromone response G protein beta gamma subunits with the MAP kinase scaffold Ste5p Science, September 15, 1995; 269(5230): 1572 - 1575. [Abstract] [PDF]
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M. Karandikar, S. Xu, and M. H. Cobb MEKK1 Binds Raf-1 and the ERK2 Cascade Components J. Biol. Chem., December 15, 2000; 275(51): 40120 - 40127. [Abstract] [Full Text] [PDF]
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