Plasma membrane proteins Slm1 and Slm2 mediate activation of the AGC kinase Ypk1 by TORC2 and sphingolipids in S. cerevisiae

Brad J. Niles, Ted Powers

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

The PH domain-containing proteins Slm1 and Slm2 were originally identifed as substrates of the rapamycin-insensitive TOR complex 2 (TORC2) and as mediators of signaling by the lipid second messenger phosphatidyl-inositol-4,5- bisphosphate (PI4,5P2) in budding yeast S. cerevisiae. More recently, these proteins have been identifed as critical effectors that facilitate phosphorylation and activation of the AGC kinases Ypk1 and Ypk2 by TORC2. 1 Here, we review the molecular basis for this regulation as well as place it within the context of recent fndings that have revealed Slm1/2 and TORC2-dependent phosphorylation of Ypk1 is coupled to the biosynthesis of complex sphingolipids and to their levels within the plasma membrane (PM), as well as other forms of PM stress. Together, these studies reveal the existence of an intricate homeostatic feedback mechanism, whereby the activity of these signaling components is linked to the biosynthesis of PM lipids according to cellular need.

Original languageEnglish (US)
Pages (from-to)3745-3749
Number of pages5
JournalCell Cycle
Volume11
Issue number20
DOIs
StatePublished - Oct 15 2012

Keywords

  • Budding yeast
  • Kinases
  • Lipids
  • Rapamycin
  • Signal transduction

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

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