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Vol. 9, Issue 6, 1339-1349, June 1998
Departments of Molecular Biology and Cell Biology, The Scripps
Research Institute, La Jolla, California 92037
Fission yeast Spc1/StyI MAPK is activated by many environmental
insults including high osmolarity, oxidative stress, and heat shock.
Spc1/StyI is activated by Wis1, a MAPK kinase (MEK), which is itself
activated by Wik1/Wak1/Wis4, a MEK kinase (MEKK). Spc1/StyI is
inactivated by the tyrosine phosphatases Pyp1 and Pyp2. Inhibition of
Pyp1 was recently reported to play a crucial role in the oxidative stress and heat shock responses. These conclusions were based on three
findings: 1) osmotic, oxidative, and heat stresses activate Spc1/StyI
in wis4 cells; 2) oxidative stress and heat shock
activate Spc1/StyI in cells that express Wis1AA, in which MEKK
consensus phosphorylation sites were replaced with alanine; and 3)
Spc1/StyI is maximally activated in 
pyp1 cells.
Contrary to these findings, we report: 1) Spc1/StyI activation by
osmotic stress is greatly reduced in wis4 cells; 2)
wis1-AA and wis1 cells have identical phenotypes; and 3) all forms of stress activate Spc1/StyI in
pyp1 cells. We also report that heat shock, but not
osmotic or oxidative stress, activate Spc1 in wis1-DD
cells, which express Wis1 protein that has the MEKK consensus
phosphorylation sites replaced with aspartic acid. Thus osmotic and
oxidative stress activate Spc1/StyI by a MEKK-dependent process,
whereas heat shock activates Spc1/StyI by a novel mechanism that does
not require MEKK activation or Pyp1 inhibition.
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