Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins

FEBS Lett. 1995 Jul 10;368(1):55-8. doi: 10.1016/0014-5793(95)00598-4.


14-3-3 proteins play a role in many cellular functions: they bind to and regulate several proteins which are critical for cell proliferation and differentiation. 14-3-3 proteins exist as dimers, and in this study we have shown that diverse 14-3-3 proteins can form both homo- and heterodimers in vitro (by cross-linking studies) and in vivo (by coimmunoprecipitation and Western blot analysis); this interaction is mediated solely through the N-terminal domain of the proteins. The composition of 14-3-3 dimers within a cell may play a key part in the role of this family of proteins as modulators or adapters which facilitate the interaction of distinct components of signalling pathways.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 14-3-3 Proteins
  • Base Sequence
  • Cell Line
  • Cloning, Molecular
  • Cross-Linking Reagents
  • Escherichia coli
  • Humans
  • Molecular Sequence Data
  • Proteins / chemistry*
  • Proteins / physiology*
  • Signal Transduction / physiology
  • Structure-Activity Relationship
  • Tyrosine 3-Monooxygenase*


  • 14-3-3 Proteins
  • Cross-Linking Reagents
  • Proteins
  • Tyrosine 3-Monooxygenase