Cyclic AMP-Dependent Protein Kinase Regulates the Subcellular Localization of Snf1-Sip1 Protein Kinase

Kristina Hedbacker, Robert Townley, Marian Carlson

Research output: Contribution to journalArticle

68 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)1836-1843
Number of pages8
JournalMolecular and cellular biology
Issue number5
StatePublished - Mar 1 2004


ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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