The heterologous interactions among plant 14-3-3 proteins and identification of regions that are important for dimerization

Arch Biochem Biophys. 1997 Mar 1;339(1):2-8. doi: 10.1006/abbi.1996.9841.


The 14-3-3 proteins constitute a family of dimeric proteins that are involved in many cellular functions. At least two mammalian 14-3-3 proteins can form heterodimers and the approximate regions important for dimerization have been identified. In this study, we demonstrate that eight Arabidopsis and one maize 14-3-3 protein can dimerize with each other and with themselves. Native gel Western analysis of Arabidopsis cell extract also suggests the presence of 14-3-3 heterodimers in vivo. Finally, we identified the domains of one 14-3-3 protein that are sufficient for homodimerization and heterodimerization. These data support the hypothesis that evolutionarily divergent 14-3-3 proteins can interact with each other to form diverse molecular modulators or adapters in signaling pathways.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • 14-3-3 Proteins
  • Amino Acid Sequence
  • Arabidopsis / chemistry*
  • Blotting, Western
  • Molecular Sequence Data
  • Molecular Weight
  • Plant Proteins / chemistry*
  • Protein Binding
  • Proteins / chemistry*
  • Recombinant Proteins
  • Saccharomyces cerevisiae
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship
  • Tyrosine 3-Monooxygenase*
  • Zea mays / chemistry*


  • 14-3-3 Proteins
  • Plant Proteins
  • Proteins
  • Recombinant Proteins
  • Tyrosine 3-Monooxygenase