Mammalian and yeast 14-3-3 isoforms form distinct patterns of dimers in vivo

Biochem Biophys Res Commun. 2003 Jan 17;300(3):679-85. doi: 10.1016/s0006-291x(02)02902-9.

Abstract

The 14-3-3 protein family associates with many proteins involved in intracellular signalling. In many cases, there is a distinct preference for a particular isoform(s) of 14-3-3. A specific repertoire of 14-3-3 dimer formation may therefore influence which of the interacting proteins could be brought together. We have analysed the pattern of dimer formation for two of the most abundant isoforms of 14-3-3, epsilon ( epsilon ) and gamma (gamma), following their stable expression. This revealed a distinct preference for particular dimer combinations that is largely independent of cellular conditions. gamma 14-3-3 occurred as homodimers and also formed heterodimers, mainly with epsilon 14-3-3 (In PC12 and Cos cells). The epsilon isoform formed heterodimers with 14-3-3 beta, gamma, zeta, and eta, but no homodimers were detected. The two 14-3-3 homologues, BMH1 and BMH2 from Saccharomyces cerevisiae, were mainly heterodimers.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 14-3-3 Proteins
  • Animals
  • Blotting, Western
  • COS Cells
  • Dimerization
  • PC12 Cells
  • Precipitin Tests
  • Protein Binding / physiology
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Protein Isoforms / metabolism
  • Rats
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Transfection
  • Tyrosine 3-Monooxygenase / chemistry
  • Tyrosine 3-Monooxygenase / genetics
  • Tyrosine 3-Monooxygenase / metabolism*

Substances

  • 14-3-3 Proteins
  • BMH1 protein, S cerevisiae
  • BMH2 protein, S cerevisiae
  • Protein Isoforms
  • Saccharomyces cerevisiae Proteins
  • Tyrosine 3-Monooxygenase