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Blood, Vol. 96 No. 2 (July 15), 2000:
pp. 577-584
Phosphoinositide 3-kinase forms a complex with platelet membrane
glycoprotein Ib-IX-V complex and 14-3-3
Adam D. Munday,
Michael C. Berndt, and
Christina
A. Mitchell
From the Department of Biochemistry and Molecular Biology, Monash
University, Clayton, and the Hazel and Pip Appel Vascular Biology
Laboratory, Baker Medical Research Institute, Prahran, Victoria,
Australia.
The binding of von Willebrand factor (vWF) to glycoprotein (GP)
Ib-IX-V stimulates transmembrane signaling events that lead to platelet
adhesion and aggregation. Recent studies have revealed that the
signaling protein 14-3-3 binds directly to the cytoplasmic domain of
GP Ib . In this study, the dynamic association of 14-3-3 with GP
Ib-IX, the phosphoinositide 3-kinase (PI 3-kinase), or both, was
investigated in resting, thrombin, or vWF and botrocetin-stimulated platelets by analysis of discrete subcellular fractions. Results of
this study demonstrate maximal coimmunoprecipitation of 14-3-3 with
GP Ib-IX in the nonstimulated cytosolic fraction and in the actin
cytoskeletal fraction of thrombin- or vWF-stimulated human platelets.
Immunoprecipitated 14-3-3 or GP Ib from cytosolic fractions
contained PI 3-kinase enzyme activity and an 85-kd polypeptide recognized by antibodies to the p85 subunit of PI 3-kinase. After platelet activation, the level of association between these species decreased in the cytosolic fraction. However, increased complex formation between 14-3-3 and GP Ib-IX and between PI
3-kinase and GP Ib-IX was detected in actin cytoskeletal fractions
derived from thrombin- or vWF-stimulated platelets. Recombinant
glutathione S-transferase-14-3-3 fusion protein
(14-3-3-GST) inhibited affinity-captured PI 3-kinase enzyme
activity up to 70% at 2 µmol/L 14-3-3-GST. However, increasing
concentrations up to 5 µmol/L 14-3-3-GST resulted in the 3-fold
enhancement of PI 3-kinase enzyme activity. We propose that the
association between PI 3-kinase and 14-3-3 with GP Ib-IX serves to
promote the rapid translocation of these signaling proteins to the
activated cytoskeleton, thereby regulating the formation of 3-position
phosphoinositide-signaling molecules in this subcellular compartment.
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