Article
- The EMBO Journal (2007) 26, 4824 - 4830
- doi:10.1038/sj.emboj.7601914
Published online: 8 November 2007
Subject Categories:
Yeast PAS kinase coordinates glucose partitioning in response to metabolic and cell integrity signaling
Julianne H Grose1, Tammy L Smith1, Hana Sabic1 and Jared Rutter1
- Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT, USA
Correspondence to:
Jared Rutter, Department of Biochemistry, University of Utah School of Medicine, 15 N Medical Drive East, Salt Lake City, UT 84112, USA. Tel.: +1 801 581 3340; Fax: +1 801 581 7959; E-mail: rutter@biochem.utah.edu
Received 22 May 2007; Accepted 17 October 2007
Abstract
PAS kinase is an evolutionarily conserved serine/threonine protein kinase. Mammalian PAS kinase is activated under nutrient replete conditions and is important for controlling metabolic rate and energy homeostasis. In yeast, PAS kinase acts to increase the synthesis of structural carbohydrate at the expense of storage carbohydrates through phosphorylation of the enzyme UDP-glucose pyrophosphorylase. We have identified two pathways that activate yeast PAS kinase; one is responsive to nutrient conditions while the other is responsive to cell integrity stress. These pathways differentially activate the two PAS kinase proteins in Saccharomyces cerevisiae, Psk1 and Psk2, with Psk1 alone responding to activation by nonfermentative carbon sources. We demonstrate that, in addition to transcriptional effects, both of these pathways post-translationally activate PAS kinase via its regulatory N-terminus. As a whole, this system acts to coordinate glucose partitioning with alterations in demand due to changes in environmental and nutrient conditions.
Keywords:
- cell integrity signaling,
- glucose metabolism,
- kinase regulation
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