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The Saccharomyces cerevisiae Spo7 basic tail is required for Nem1-Spo7/Pah1 phosphatase cascade function in lipid

Ruta Jog1, Gil-Soo Han1, George M Carman1

  • 1Department of Food Science and the Rutgers Center for Lipid Research, New Jersey Institute for Food, Nutrition, and Health, Rutgers University, New Brunswick, New Jersey, USA.

The Journal of Biological Chemistry
|December 23, 2023
PubMed
Summary

The Spo7 protein

Keywords:
Nem1Pah1Saccharomyces cerevisiaeSpo7diacylglycerollipid dropletmembranephosphatidate phosphatasephospholipidprotein phosphatasetriacylglycerolyeast

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • The Nem1-Spo7 complex regulates Pah1, a key enzyme in yeast lipid metabolism.
  • Pah1 dephosphorylates phosphatidate to generate diacylglycerol, essential for triacylglycerol synthesis and lipid droplet formation.
  • Dysregulation of this pathway leads to significant physiological defects in yeast.

Purpose of the Study:

  • To identify the specific region of Spo7 responsible for interacting with Pah1.
  • To elucidate the role of this interaction in the Nem1-Spo7/Pah1 phosphatase cascade.
  • To understand how this interaction impacts cellular functions related to lipid metabolism and cell growth.

Main Methods:

  • Deletion and site-specific mutational analyses of the Spo7 protein.
  • Glutaraldehyde cross-linking analysis of synthetic peptides.
  • Assessment of cellular functions including triacylglycerol synthesis, lipid droplet formation, membrane morphology, and cell growth.

Main Results:

  • The C-terminal basic tail of Spo7 (residues 240-259) is crucial for Pah1 dephosphorylation and activation.
  • This basic tail of Spo7 directly interacts with the acidic tail of Pah1.
  • Spo7's C-terminal tail is essential for regulating triacylglycerol synthesis, lipid droplet formation, nuclear/ER membrane integrity, and thermotolerance.

Conclusions:

  • The C-terminal basic tail of Spo7 is identified as the key region for Pah1 interaction.
  • This interaction is critical for the proper functioning of the Nem1-Spo7/Pah1 phosphatase cascade in yeast.
  • The findings deepen the understanding of yeast lipid metabolism regulation and the roles of Spo7 and Pah1.