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Genes & Dev. 15 (9): 1104-1114
Copyright © 2001 by Cold Spring Harbor Laboratory Press.
Vol. 15, No. 9, pp. 1104-1114, May 1, 2001
RESEARCH PAPER
Subcellular localization of the Snf1 kinase is regulated by specific subunits and a novel glucose signaling mechanism
Olivier
Vincent,1
Robert
Townley,2
Sergei
Kuchin,1 and
Marian
Carlson1,2,3
1 Departments of Genetics and Development and Microbiology,
and 2 Integrated Program in Cellular Biology, Molecular
Biology and Biophysical Studies, Columbia University,
New York, New York 10032, USA
The Snf1/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
(catalytic) subunit Snf1, one of the three related subunits
Gal83, Sip1, or Sip2, and the subunit Snf4. We present evidence
that the 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 subunits,
affords versatility in regulating physiological responses.
[Key Words:
Snf1/AMPK kinases; yeast; nuclear
localization; glucose signaling]
3
Corresponding author.
GENES & DEVELOPMENT 15:1104-1114 © 2001 by Cold Spring Harbor Laboratory Press ISSN 0890-9369/01 $5.00
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