Lk. Taylor et al., NEWLY IDENTIFIED STRESS-RESPONSIVE PROTEIN-KINASES, KRS-1 AND KRS-2, Proceedings of the National Academy of Sciences of the United Statesof America, 93(19), 1996, pp. 10099-10104
The activation of protein kinases is a frequent response of cells to t
reatment with growth factors, chemicals, heat shock, or apoptosis-indu
cing agents. However, when several agents result in the activation of
the same enzymes, it is unclear how specific biological responses are
generated. We describe here two protein kinases that are activated by
a subset of stress conditions or apoptotic agents but are not activate
d by commonly used mitogenic stimuli. Purification and cloning demonst
rate that these protein kinases are members of a subfamily of kinases
related to Ste20p, a serine/threonine kinase that functions early in a
pheromone responsive signal transduction cascade in yeast. The specif
icity of Krs-1 and Krs-2 activation and their similarity to Ste20p sug
gest that they may function at an early step in phosphorylation events
that are specific responses to some forms of chemical stress or extre
me heat shock.