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Papers In Press, published online ahead of print April 19, 2005
Molecular and Cellular Biochemistry, Univ. of Kentucky College of Medicine, Lexington, KY 40536
Corresponding Author: bobd{at}uky.edu
The Pkh1 protein kinase of Saccharomyces cerevisiae, a homolog of the mammalian 3-phosphoinositide-dependent kinase (PDK1), regulates downstream AGC kinases including Ypk1/2 and Pkc1, which control cell wall integrity, growth and other processes. Phytosphingosine (PHS), a sphingoid long chain base, is hypothesized to be a lipid activator of Pkh1 and thereby control the activity of Ypk1/2. Here we present biochemical evidence supporting this hypothesis and, in addition, we demonstrate that PHS also stimulates autophosphorylation and activation of Ypk1/2. Greatest stimulation of Ypk1/2 phosphorylation and activity are achieved by inclusion of both PHS and Pkh1 in an in vitro kinase reaction. We also demonstrate for the first time that Pkh1 phosphorylates the Sch9 protein kinase in vitro and that such phosphorylation is stimulated by PHS. This is the first biochemical demonstration of Sch9 activators and the results further support roles for LCBs in heat stress resistance, in addition to implying roles in chronological aging and cell size determination, since Sch9 functions in these processes. Thus, our data support a model in which PHS, rather than simply being an upstream activator of Pkh1, also activates kinases that are downstream targets of Pkh1 including Ypk1/2 and Sch9.
J. Biol. Chem, 10.1074/jbc.M502972200
Submitted on March 17, 2005
Revised on April 15, 2005
Accepted on April 19, 2005
The sphingolipid long chain base phytosphingosine activates AGC kinases in Saccharomyces cerevisiae including Ypk1, Ypk2 and Sch9
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