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Human Signaling Protein 14-3-3 Interacts With Platelet
Glycoprotein Ib Subunits Ib and Ib
David C. Calverley,
Terrance J. Kavanagh, and
Gerald J. Roth
From the Medical and Research Services, Seattle Veterans'
Affairs Medical Center, Seattle; and the Division of
Hematology, Department of Medicine, and Department of Environmental
Health, University of Washington, Seattle, WA.
The initiation of primary hemostasis is mediated by interaction of
the platelet glycoprotein Ib (GPIb) surface receptor and its arterial
subendothelial von Willebrand factor (vWF) ligand. The intracellular
signaling immediately following GPIb receptor occupancy connecting the
adhesive event to platelet activation and aggregation has not been well
characterized. The 14-3-3 proteins are a 27- to 30-kD ubiquitous
protein family with diverse biologic roles, including functional
modulation of several prominent signaling proteins. We used the yeast
two-hybrid system and confocal microscopy to characterize the recently
described interaction between GPIb and platelet 14-3-3 , and provide
evidence for the potential signaling role of this protein. Two-hybrid
interactions suggest that platelet 14-3-3 associates with the
cytoplasmic domain of GPIb subunits Ib and Ib in transformed
yeast cells. The 14-3-3 interaction with GPIb may be partly mediated
through the latter's phosphorylated serine 166 residue as its
mutagenesis results in 20% to 40% reduced interaction. There was 51%
to 59% reduced interaction between GPIb and three 14-3-3 deletion
mutants compared with full-length 14-3-3, suggesting that either the
N-terminal dimerization or membrane-binding domains or more
than one noncontiguous 14-3-3 element may be required for optimal
GPIb interaction. Confocal studies of platelets and a megakaryocyte
cell line provided additional evidence for interaction of 14-3-3
with GPIb and GPIb. We also found that, similar to the signaling
mediators phosphatidylinositol 3-kinase and Src, platelet cytoskeletal
14-3-3 content is increased following vWF and ristocetin
stimulation. We suggest that platelet 14-3-3 interacts with GPIb
and Ib, that this interaction may be partly mediated through
phosphoserine recognition, and that 14-3-3 cytoskeletal
translocation may serve as a GPIb post-receptor occupancy signaling
event.
Blood, Vol. 91 No. 4 (February 15), 1998:
pp. 1295-1303
© 1998 by The American Society of Hematology.
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