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Blood, Vol. 95 No. 2 (January 15), 2000:
pp. 551-557
Cytoplasmic domains of GpIb and GpIb regulate 14-3-3
binding to GpIb/IX/V
Shuju Feng,
Nicolaos Christodoulides,
Julio C. Reséndiz,
Michael C. Berndt, and
Michael H. Kroll
From the Veterans Administration Medical Center, Baylor College of
Medicine and Rice University, Houston, TX, and the Baker Medical
Research Institute, Prahran, Victoria, Australia.
Shear stress causes the platelet glycoprotein (Gp) Ib/IX/V to bind
to von Willebrand factor, resulting in platelet adhesion. GpIb/IX/V
also functions to stimulate transmembranous signaling, leading to
platelet activation and the expression of a ligand-receptive GpIIb-IIIa
complex. The highly conserved cytoplasmic domain of GpIb binds
directly to a dimeric 14-3-3 adapter protein  isoform. To explore
structural determinants of GpIb/IX/V binding to 14-3-3, the authors
examined 14-3-3 interactions with GpIb and GpIb in
heterologous cells and platelets. Truncations of GpIb at amino acid
542 or 594, or deletions of residues 542 through 590, inhibited binding
of 14-3-3. Deletion of GpIb from Trp570 to
Ser590 eliminated 14-3-3 binding, and deletion of the
sequence from Arg542-Trp570 enhanced binding of
14-3-3 to GpIb. All GpIb mutations that eliminated GpIb
binding to the GST-14-3-3 fusion protein also eliminated GpIb
binding to the fusion protein. Forskolin treatment of Chinese hamster
ovary cells expressing wild-type GpIb//IX resulted in the
phosphorylation of GpIb associated with enhanced binding of GpIb
to GST-14-3-3 fusion protein and increased 14-3-3 coimmunoprecipitated with GpIb. When intact human platelets
aggregated in response to 90 dynes/cm2 shear stress,
14-3-3 disassociated from GpIb. Prostacyclin treatment of
platelets inhibited shear stress-induced aggregation and the release of
14-3-3 from GpIb. These data demonstrate that amino acid residues
in the cytoskeletal interaction domains of GpIb regulate 14-3-3
binding to GpIb//IX, and suggest that protein kinase A-dependent
phosphorylation of GpIb enhances 14-3-3 binding to the GpIb/IX/V
complex in human platelets.
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