The requirement for the hydrophobic motif phosphorylation of Ypk1 in yeast differs depending on the downstream events, including endocytosis, cell growth, and resistance to a sphingolipid biosynthesis inhibitor, ISP-1.

Abstract

ISP-1 inhibits de novo sphingolipid biosynthesis and induces growth defects in both mammals and yeast (Saccharomyces cerevisiae). In our previous study, YPK1/SLI2 was identified as one of multicopy suppressor genes for ISP-1 in yeast. Ypk1 is proposed to be a downstream serine/threonine kinase of the sphingolipid signaling pathway in yeast. Other than… (More)

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Cite this paper

@article{Tanoue2005TheRF, title={The requirement for the hydrophobic motif phosphorylation of Ypk1 in yeast differs depending on the downstream events, including endocytosis, cell growth, and resistance to a sphingolipid biosynthesis inhibitor, ISP-1.}, author={Daisuke Tanoue and Takafumi Kobayashi and Yidi Sun and Tetsuro Fujita and Hiromu Takematsu and Yasunori Kozutsumi}, journal={Archives of biochemistry and biophysics}, year={2005}, volume={437 1}, pages={29-41} }