TY - JOUR
T1 - Subcellular localization of the Snf1 kinase is regulated by specific β subunits and a novel glucose signaling mechanism
AU - Vincent, Olivier
AU - Townley, Robert
AU - Kuchin, Sergei
AU - Carlson, Marian
PY - 2001/5/1
Y1 - 2001/5/1
N2 - The Snfl/AMP-activated protein kinase family has broad roles in transcriptional, metabolic, and developmental regulation in response to stress. In Saccharomyces cerevisiae, Snf1 is required for the response to glucose limitation. Snf1 kinase complexes contain the α (catalytic) subunit Snf1, one of the three related β subunits Gal83, Sip1, or Sip2, and the γ subunit Snf4. We present evidence that the β subunits regulate the subcellular localization of the Snf1 kinase. Green fluorescent protein fusions to Gal83, Sip1, and Sip2 show different patterns of localization to the nucleus, vacuole, and/or cytoplasm. We show that Gal83 directs Snf1 to the nucleus in a glucose-regulated manner. We further identify a novel signaling pathway that controls this nuclear localization in response to glucose phosphorylation. This pathway is distinct from the glucose signaling pathway that inhibits Snf1 kinase activity and responds not only to glucose but also to galactose and sucrose. Such independent regulation of the localization and the activity of the Snf1 kinase, combined with the distinct localization of kinases containing different β subunits, affords versatility in regulating physiological responses.
AB - The Snfl/AMP-activated protein kinase family has broad roles in transcriptional, metabolic, and developmental regulation in response to stress. In Saccharomyces cerevisiae, Snf1 is required for the response to glucose limitation. Snf1 kinase complexes contain the α (catalytic) subunit Snf1, one of the three related β subunits Gal83, Sip1, or Sip2, and the γ subunit Snf4. We present evidence that the β subunits regulate the subcellular localization of the Snf1 kinase. Green fluorescent protein fusions to Gal83, Sip1, and Sip2 show different patterns of localization to the nucleus, vacuole, and/or cytoplasm. We show that Gal83 directs Snf1 to the nucleus in a glucose-regulated manner. We further identify a novel signaling pathway that controls this nuclear localization in response to glucose phosphorylation. This pathway is distinct from the glucose signaling pathway that inhibits Snf1 kinase activity and responds not only to glucose but also to galactose and sucrose. Such independent regulation of the localization and the activity of the Snf1 kinase, combined with the distinct localization of kinases containing different β subunits, affords versatility in regulating physiological responses.
KW - Glucose signaling
KW - Nuclear localization
KW - Snfl/AMPK kinases
KW - Yeast
UR - http://www.scopus.com/inward/record.url?scp=0035338114&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035338114&partnerID=8YFLogxK
U2 - 10.1101/gad.879301
DO - 10.1101/gad.879301
M3 - Article
C2 - 11331606
AN - SCOPUS:0035338114
SN - 0890-9369
VL - 15
SP - 1104
EP - 1114
JO - Genes and Development
JF - Genes and Development
IS - 9
ER -