14-3-3 proteins in platelet biology and glycoprotein Ib-IX signaling

Blood. 2018 May 31;131(22):2436-2448. doi: 10.1182/blood-2017-09-742650. Epub 2018 Apr 5.

Abstract

Members of the 14-3-3 family of proteins function as adapters/modulators that recognize phosphoserine/phosphothreonine-based binding motifs in many intracellular proteins and play fundamental roles in signal transduction pathways of eukaryotic cells. In platelets, 14-3-3 plays a wide range of regulatory roles in phosphorylation-dependent signaling pathways, including G-protein signaling, cAMP signaling, agonist-induced phosphatidylserine exposure, and regulation of mitochondrial function. In particular, 14-3-3 interacts with several phosphoserine-dependent binding sites in the major platelet adhesion receptor, the glycoprotein Ib-IX complex (GPIb-IX), regulating its interaction with von Willebrand factor (VWF) and mediating VWF/GPIb-IX-dependent mechanosignal transduction, leading to platelet activation. The interaction of 14-3-3 with GPIb-IX also plays a critical role in enabling the platelet response to low concentrations of thrombin through cooperative signaling mediated by protease-activated receptors and GPIb-IX. The various functions of 14-3-3 in platelets suggest that it is a possible target for the treatment of thrombosis and inflammation.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • 14-3-3 Proteins / metabolism*
  • Animals
  • Blood Coagulation
  • Blood Platelets / cytology
  • Blood Platelets / metabolism*
  • Humans
  • Phosphorylation
  • Platelet Activation*
  • Platelet Glycoprotein GPIb-IX Complex / metabolism*
  • Protein Binding
  • Signal Transduction*
  • von Willebrand Factor / metabolism

Substances

  • 14-3-3 Proteins
  • Platelet Glycoprotein GPIb-IX Complex
  • von Willebrand Factor