Regulation of sphingolipid biosynthesis in the endoplasmic reticulum via signals from the plasma membrane in budding yeast

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  • Yuko Ishino
    Department of Applied Biological Science Faculty of Agriculture Kagawa University Miki‐cho Japan
  • Nao Komatsu
    Department of Applied Biological Science Faculty of Agriculture Kagawa University Miki‐cho Japan
  • Ken‐taro Sakata
    Department of Applied Biological Science Faculty of Agriculture Kagawa University Miki‐cho Japan
  • Daichi Yoshikawa
    Department of Applied Biological Science Faculty of Agriculture Kagawa University Miki‐cho Japan
  • Motohiro Tani
    Department of Chemistry Faculty of Sciences Kyushu University Fukuoka Japan
  • Tatsuya Maeda
    Department of Biology Hamamatsu University School of Medicine Japan
  • Kanta Morishige
    Department of Applied Biological Science Faculty of Agriculture Kagawa University Miki‐cho Japan
  • Koushiro Yoshizawa
    Department of Applied Biological Science Faculty of Agriculture Kagawa University Miki‐cho Japan
  • Naotaka Tanaka
    Department of Applied Biological Science Faculty of Agriculture Kagawa University Miki‐cho Japan
  • Mitsuaki Tabuchi
    Department of Applied Biological Science Faculty of Agriculture Kagawa University Miki‐cho Japan

抄録

<jats:p><jats:italic>Saccharomyces cerevisiae LIP1</jats:italic> encodes a regulatory subunit that forms a complex with the ceramide synthase catalytic subunits, Lag1/Lac1, which is localized on the membrane of endoplasmic reticulum. To understand the underlying regulatory mechanism of sphingolipid biosynthesis, we generated strains upon replacing the chromosomal <jats:italic>LIP1</jats:italic> promoter with a Tet‐off promoter, which enables the expression in Dox‐dependent manner. The <jats:italic>lip1‐1</jats:italic> strain, obtained through the promoter substitution, exhibits severe growth inhibition and remarkable decrease in sphingolipid synthesis in the presence of Dox. Using this strain, we investigated the effect of a decrease in ceramide synthesis on TOR complex 2 (TORC2)‐Ypk1 signaling, which senses the complex sphingolipid level at the plasma membrane and promotes sphingolipid biosynthesis. In <jats:italic>lip1‐1</jats:italic> cells, Ypk1 was activated via both upstream kinases, TORC2 and yeast PDK1 homologues, Pkh1/2, thereby inducing hyperphosphorylation of Lag1, but not of another Ypk1‐substrate, Orm1, which is a known negative regulator of the first step of sphingolipid metabolism, in the presence of Dox. Therefore, our data suggest that the metabolic enzyme activities at each step of the sphingolipid biosynthetic pathway are controlled through a fine regulatory mechanism.</jats:p>

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