14-3-3 proteins--an update

Cell Res. 2005 Apr;15(4):228-36. doi: 10.1038/sj.cr.7290291.

Abstract

14-3-3 is a highly conserved acidic protein family, composed of seven isoforms in mammals. 14-3-3 protein can interact with over 200 target proteins by phosphoserine-dependent and phosphoserine-independent manners. Little is known about the consequences of these interactions, and thus are the subjects of ongoing studies. 14-3-3 controls cell cycle, cell growth, differentiation, survival, apoptosis, migration and spreading. Recent studies have revealed new mechanisms and new functions of 14-3-3, giving us more insights on this fascinating and complex family of proteins. Of all the seven isoforms, 14-3-3sigma seems to be directly involved in human cancer. 14-3-3sigma itself is subject to regulation by p53 upon DNA damage and by epigenetic deregulation. Gene silencing of 14-3-3sigma by CpG methylation has been found in many human cancer types. This suggests that therapy-targeting 14-3-3sigma may be beneficial for future cancer treatment.

Publication types

  • Review

MeSH terms

  • 14-3-3 Proteins* / metabolism
  • 14-3-3 Proteins* / pharmacology
  • 14-3-3 Proteins* / physiology
  • Animals
  • Biomarkers, Tumor / antagonists & inhibitors
  • Biomarkers, Tumor / genetics
  • Biomarkers, Tumor / metabolism
  • Cell Cycle / drug effects
  • Cell Differentiation / drug effects
  • Cell Proliferation / drug effects
  • Cell Survival / drug effects
  • CpG Islands / genetics
  • Enzyme Inhibitors / pharmacology
  • Exonucleases / antagonists & inhibitors
  • Exonucleases / genetics
  • Exonucleases / metabolism
  • Exoribonucleases
  • Humans
  • Isoenzymes
  • Neoplasm Proteins / antagonists & inhibitors
  • Neoplasm Proteins / genetics
  • Neoplasm Proteins / metabolism
  • Neoplasms / genetics
  • Phosphoserine / metabolism
  • Protein Binding

Substances

  • 14-3-3 Proteins
  • Biomarkers, Tumor
  • Enzyme Inhibitors
  • Isoenzymes
  • Neoplasm Proteins
  • Phosphoserine
  • Exonucleases
  • Exoribonucleases
  • SFN protein, human