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- W2114586171 endingPage "1843" @default.
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- W2114586171 abstract "ABSTRACT The Snf1/AMP-activated protein kinase family has diverse roles in cellular responses to metabolic stress. In Saccharomyces cerevisiae , Snf1 protein kinase has three isoforms of the β subunit that confer versatility on the kinase and that exhibit distinct patterns of subcellular localization. The Sip1 β subunit resides in the cytosol in glucose-grown cells and relocalizes to the vacuolar membrane in response to carbon stress. We show that translation of Sip1 initiates at the second ATG of the open reading frame, yielding a potential site for N myristoylation, and that mutation of the critical glycine abolishes relocalization. We further show that the cyclic AMP-dependent protein kinase (protein kinase A [PKA]) pathway maintains the cytoplasmic localization of Sip1 in glucose-grown cells. The Snf1 catalytic subunit also exhibits aberrant localization to the vacuolar membrane in PKA-deficient cells, indicating that PKA regulates the localization of Snf1-Sip1 protein kinase. These findings establish a novel mechanism of regulation of Snf1 protein kinase by the PKA pathway." @default.
- W2114586171 created "2016-06-24" @default.
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- W2114586171 creator A5063445976 @default.
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- W2114586171 date "2004-03-01" @default.
- W2114586171 modified "2023-10-15" @default.
- W2114586171 title "Cyclic AMP-Dependent Protein Kinase Regulates the Subcellular Localization of Snf1-Sip1 Protein Kinase" @default.
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- W2114586171 doi "https://doi.org/10.1128/mcb.24.5.1836-1843.2004" @default.
- W2114586171 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/350547" @default.
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