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Vol. 9, Issue 2, 311-322, February 1998
Division of Yeast Genetics, National Institute for Medical
Research, The Ridgeway, Mill Hill, London NW7 1AA, United Kingdom
The fission yeast Sty1 mitogen-activated protein (MAP) kinase
(MAPK) and its activator the Wis1 MAP kinase kinase (MAPKK) are
required for cell cycle control, initiation of sexual differentiation, and protection against cellular stress. Like the mammalian JNK/SAPK and
p38/CSBP1 MAPKs, Sty1 is activated by a range of environmental insults
including osmotic stress, hydrogen peroxide, UV light, menadione, heat
shock, and the protein synthesis inhibitor anisomycin. We have recently
identified two upstream regulators of the Wis1 MAPKK, namely the Wak1
MAPKKK and the Mcs4 response regulator. Cells lacking Mcs4 or Wak1,
however, are able to proliferate under stressful conditions and undergo
sexual differentiation, suggesting that additional pathway(s) control
the Wis1 MAPKK. We now show that this additional signal information is
provided, at least in part, by the Win1 mitotic regulator. We show that
Wak1 and Win1 coordinately control activation of Sty1 in response to
multiple environmental stresses, but that Wak1 and Win1 perform
distinct roles in the control of Sty1 under poor nutritional
conditions. Our results suggest that the stress-activated Sty1 MAPK
integrates information from multiple signaling pathways.
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