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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 beta  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 alpha  (catalytic) subunit Snf1, one of the three related beta  subunits Gal83, Sip1, or Sip2, and the gamma  subunit Snf4. We present evidence that the beta  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 beta  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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