Identification of a binding sequence for the 14-3-3 protein within the cytoplasmic domain of the adhesion receptor, platelet glycoprotein Ib alpha.

The zeta-form 14-3-3 protein (14-3-3zeta) regulates protein kinases and interacts with several signaling molecules. We reported previously that a platelet adhesion receptor, glycoprotein (GP) Ib-IX, was associated with a 29-kDa protein with partial sequences identical to 14-3-3zeta. In this study, the interaction between GPIb-IX and recombinant 14-3-3zeta is reconstituted. Further, ...
we show that the 14-3-3zeta binding site in GPIb is within a 15 residue sequence at the C terminus of GPIb-alpha, as indicated by antibody inhibition and direct binding of 14-3-3zeta to synthetic GPIb-alpha cytoplasmic domain peptides. The 14-3-3zeta binds to recombinant wild type GPIb-IX but not to the GPIb-alpha mutants lacking C-terminal 5 or more residues, suggesting that the C-terminal 5 residues of GPIb-alpha are critical. Similarity between the GPIb-alpha C-terminal sequence and the serine-rich regions of Raf and Bcr kinases suggests a possible serine-rich recognition motif for the 14-3-3 protein.
Mesh Terms:
14-3-3 Proteins, Amino Acid Sequence, Animals, Antibodies, Base Sequence, Binding Sites, CHO Cells, Cell Line, Chromatography, Affinity, Cloning, Molecular, Cricetinae, DNA Primers, Electrophoresis, Polyacrylamide Gel, Gene Library, Humans, Immunoblotting, Kinetics, Molecular Sequence Data, Peptides, Platelet Glycoprotein GPIb-IX Complex, Polymerase Chain Reaction, Protein Conformation, Proteins, Recombinant Proteins, Sequence Homology, Amino Acid, Serine, Signal Transduction, Transfection, Tumor Cells, Cultured, Tyrosine 3-Monooxygenase
J. Biol. Chem.
Date: Mar. 29, 1996
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