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Vol. 10, Issue 7, 2425-2440, July 1999
Eukaryotic Genetics Group, Biotechnology Research Institute,
National Research Council of Canada, Montreal, Quebec H4P 2R2, Canada
The Saccharomyces cerevisiae Ste11p protein kinase
is a homologue of mammalian MAPK/extracellular signal-regulated
protein kinase kinase kinases (MAPKKKs or MEKKs) as well as the
Schizosaccharomyces pombe Byr2p kinase. Ste11p functions
in several signaling pathways, including those for mating pheromone
response and osmotic stress response. The Ste11p kinase has an
N-terminal domain that interacts with other signaling molecules to
regulate Ste11p function and direct its activity in these pathways. One
of the Ste11p regulators is Ste50p, and Ste11p and Ste50p associate
through their respective N-terminal domains. This interaction relieves
a negative activity of the Ste11p N terminus, and removal of this
negative function is required for Ste11p function in the
high-osmolarity glycerol (HOG) pathway. The Ste50p/Ste11p interaction
is also important (but not essential) for Ste11p function in the mating
pathway; in this pathway binding of the Ste11p N terminus with both
Ste50p and Ste5p is required, with the Ste5p association playing the major role in Ste11p function. In vitro, Ste50p disrupts an association between the catalytic C terminus and the regulatory N terminus of
Ste11p. In addition, Ste50p appears to modulate Ste11p
autophosphorylation and is itself a substrate of the Ste11p kinase.
Therefore, both in vivo and in vitro data support a role for Ste50p in
the regulation of Ste11p activity.
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