The 14-3-3 proteins positively regulate rapamycin-sensitive signaling

Curr Biol. 1998 Nov 19;8(23):1259-67. doi: 10.1016/s0960-9822(07)00535-0.

Abstract

Background: The kinase Tor is the target of the immunosuppressive drug rapamycin and is a member of the phosphatidylinositol kinase (PIK)-related kinase family. It plays an essential role in progression through the G1 phase of the cell cycle. The molecular details of Tor signaling remain obscure, however.

Results: We isolated two Saccharomyces cerevisiae genes, BMH1 and BMH2, as multicopy suppressors of the growth-inhibitory phenotype caused by rapamycin in budding yeast. BMH1 and BMH2 encode homologs of the 14-3-3 signal transduction proteins. Deletion of one or both BMH genes caused hypersensitivity to rapamycin in a manner that was dependent on gene dosage. In addition, alterations in the phosphopeptide-binding pocket of the 14-3-3 proteins had dramatically different effects on their ability to relieve the growth-arresting rapamycin phenotype. Mutations that prevented 14-3-3 from binding to a phosphoserine motif abolished its ability to confer rapamycin resistance. In contrast, substitution of two residues in 14-3-3 that surround these phosphoserine-binding sites conferred a dominant rapamycin-resistant phenotype.

Conclusions: Our studies reveal 14-3-3 as an important component in rapamycin-sensitive signaling and provide significant new insights into the structure and function of 14-3-3 proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 14-3-3 Proteins
  • Binding Sites
  • Drug Resistance, Microbial
  • Enzyme Inhibitors / pharmacology
  • Female
  • Fungal Proteins / antagonists & inhibitors
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Fungal Proteins / physiology*
  • Genes, Fungal
  • Humans
  • Immunophilins / metabolism
  • Ligands
  • Phosphatidylinositol 3-Kinases*
  • Phosphoserine / metabolism
  • Phosphotransferases (Alcohol Group Acceptor) / antagonists & inhibitors
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism
  • Proteins / genetics
  • Proteins / physiology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins*
  • Signal Transduction* / drug effects
  • Sirolimus / antagonists & inhibitors
  • Sirolimus / pharmacology
  • Tacrolimus Binding Proteins
  • Tyrosine 3-Monooxygenase*

Substances

  • 14-3-3 Proteins
  • BMH1 protein, S cerevisiae
  • BMH2 protein, S cerevisiae
  • Enzyme Inhibitors
  • Fungal Proteins
  • Ligands
  • Proteins
  • Saccharomyces cerevisiae Proteins
  • Phosphoserine
  • Tyrosine 3-Monooxygenase
  • Phosphotransferases (Alcohol Group Acceptor)
  • TOR1 protein, S cerevisiae
  • Tacrolimus Binding Proteins
  • Immunophilins
  • Sirolimus