Proteomic analysis of in vivo 14-3-3 interactions in the yeast Saccharomyces cerevisiae

Biochemistry. 2007 Jul 3;46(26):7781-92. doi: 10.1021/bi700501t. Epub 2007 Jun 9.


The yeast Saccharomyces cerevisiae produces two 14-3-3 proteins, Bmh1 and Bmh2, whose exact functions have remained unclear. Here, we performed a comprehensive proteomic analysis using multistep immunoaffinity purification and mass spectrometry and identified 271 yeast proteins that specifically bind to Bmh1 and -2 in a phosphorylation-dependent manner. The identified proteins have diverse biochemical functions and cellular roles, including cell signaling, metabolism, and cell cycle regulation. Importantly, there are a number of protein subsets that are involved in the regulation of yeast physiology through a variety of cell signaling pathways, including stress-induced transcription, cell division, and chitin synthesis at the cell wall. In fact, we found that a yeast mutant deficient in Bmh1 and -2 had defects in signal-dependent response of the MAPK (Hog1 and Mpk1) cascade and exhibited an abnormal accumulation of chitin at the bud neck. We propose that Bmh1 and -2 are common regulators of many cell signaling modules and pathways mediated by protein phosphorylation and regulate a variety of biological events by coordinately controlling the identified multiplex phosphoprotein components.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 14-3-3 Proteins / metabolism*
  • Chitin / biosynthesis
  • Mitogen-Activated Protein Kinases / physiology
  • Protein Binding
  • Proteomics / methods*
  • Saccharomyces cerevisiae / physiology*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Saccharomyces cerevisiae Proteins / physiology
  • Signal Transduction / physiology


  • 14-3-3 Proteins
  • BMH1 protein, S cerevisiae
  • BMH2 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Chitin
  • HOG1 protein, S cerevisiae
  • Mitogen-Activated Protein Kinases
  • SLT2 protein, S cerevisiae