Growth control of golgi phosphoinositides by reciprocal localization of sac1 lipid phosphatase and pik1 4-kinase

Frank Faulhammer, Suparna Kanjilal-Kolar, Andreas Knödler, Jennifer Lo, Yerim Lee, Gerlinde Konrad, Peter Mayinger

Research output: Contribution to journalArticlepeer-review

65 Scopus citations


Compartment-specific control of phosphoinositide lipids is essential for cell function. The Sac1 lipid phosphatase regulates endoplasmic reticulum (ER) and Golgi phosphatidylinositol-4-phosphate [PI(4)P] in response to nutrient levels and cell growth stages. During exponential growth, Sac1p interacts with Dpm1p at the ER but shuttles to the Golgi during starvation. Here, we report that a C-terminal region in Sac1p is required for retention in the perinuclear ER, whereas the N-terminal domain is responsible for Golgi localization. We also show that starvation-induced shuttling of Sac1p to the Golgi depends on the coat protein complex II and the Rer1 adaptor protein. Starvation-induced shuttling of Sac1p to the Golgi specifically eliminates a pool of PI(4)P generated by the lipid kinase Pik1p. In addition, absence of nutrients leads to a rapid dissociation of Pik1p, together with its non-catalytical subunit Frq1p, from Golgi membranes. Reciprocal rounds of association/dissociation of the Sac1p lipid phosphatase and the Pik1p/ Frq1p lipid kinase complex are responsible for growth-dependent control of Golgi phosphoinositides. Sac1p and Pik1p/Frq1p are therefore elements of a unique machinery that synchronizes ER and Golgi function in response to different growth conditions.

Original languageEnglish (US)
Pages (from-to)1554-1567
Number of pages14
Issue number11
StatePublished - Nov 2007


  • Cell growth
  • Endoplasmic reticulum
  • Golgi apparatus
  • Phosphoinositides
  • Pik1p
  • Rer1p
  • Sac1p

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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