Protein Chemistry and Structure
Identification of a Binding Sequence for the 14-3-3 Protein within the Cytoplasmic Domain of the Adhesion Receptor, Platelet Glycoprotein Ibα (∗)

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The ζ-form 14-3-3 protein (14-3-3ζ) 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 14-3-3ζ. In this study, the interaction between GPIb-IX and recombinant 14-3-3ζ is reconstituted. Further, we show that the 14-3-3ζ binding site in GPIb is within a 15 residue sequence at the C terminus of GPIbα, as indicated by antibody inhibition and direct binding of 14-3-3ζ to synthetic GPIbα cytoplasmic domain peptides. The 14-3-3ζ binds to recombinant wild type GPIb-IX but not to the GPIbα mutants lacking C-terminal 5 or more residues, suggesting that the C-terminal 5 residues of GPIbα are critical. Similarity between the GPIbα 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.

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∗

This work was supported by Grants HL52547 (to X. D.) and HL30657 (to J. E. F.) from the National Institutes of Health. This is Publication 9624-VB from The Scripps Research Institute. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore by hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

© 1996 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.