The pathway by which the yeast protein kinase Snf1p controls acquisition of sodium tolerance is different from that mediating glucose regulation

Derepression Snf3
DOI: 10.1099/mic.0.2008/020149-0 Publication Date: 2008-08-30T01:46:31Z
ABSTRACT
It recently became apparent that the highly conserved Snf1p protein kinase plays roles in controlling different cellular processes yeast Saccharomyces cerevisiae, addition to its well-known function glucose repression/derepression. We have previously reported together with Gis4p controls ion homeostasis by regulating expression of ENA1, which encodes Ena1p Na(+) extrusion system. In this study we found is rapidly phosphorylated when cells are exposed NaCl and phosphorylation required for role tolerance. contrast activation low levels, salt-induced promoted neither nor nuclear export Mig1p repressor. The mechanism prevents active under salt stress does not involve either hexokinase PII or regulator. Instead, may mediate upregulation ENA1 via repressor Nrg1p. Activation response depletion requires any three upstream kinases Sak1p, Tos3p Elm1p, Sak1p playing most prominent role. same were phosphorylation, also these conditions played Unexpectedly, however, it appears Elm1p a dual acquisition tolerance activating presently unknown parallel pathway. Together, results indicate takes part pathway from during performed as well Elm1p. be wider functional network than anticipated full complexity remains elucidated.
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