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J Biol Chem, Vol. 274, Issue 4, 1914-1919, January 22, 1999

Phosphorylation Sites in the Integrin beta 3 Cytoplasmic Domain in Intact Platelets

Kenneth M. Lerea, Kenneth P. Cordero, Kjell S. Sakariassen§, Rita I. Kirk, and Victor A. Fried

From the Department of Cell Biology and Anatomy, New York Medical College, Valhalla, New York 10595 and the § Department of Biology, University of Oslo, 0317 Oslo, Norway

Protein seryl/threonyl phosphatase inhibitors such as calyculin A block inside-out and outside-in platelet signaling. Our studies demonstrate that the addition of calyculin A blocks platelet adhesion and spreading on fibrinogen, responses that depend on integrin alpha IIbbeta 3 signaling. We hypothesized that this reflects a change in alpha IIbbeta 3 structure caused by a specific state of phosphorylation. We show that addition of calyculin A leads to increased phosphorylation of the beta 3 subunit, and phosphoamino acid analysis reveals that only threonine residues become phosphorylated; sequence analysis by Edman degradation established that threonine 753 became stoichiometrically phosphorylated during inhibition of platelet phosphatases by calyculin A. This region of beta 3 is linked to outside-in signaling such as platelet spreading responses. The effect of calyculin A on platelet adhesion and spreading and on the phosphorylation of T-753 in beta 3 is reversed by the calcium ionophore A23187, demonstrating that these effects of calyculin A are not generally toxic ones. We propose that phosphorylation of beta 3 on threonine 753, a region of beta 3 linked to outside-in signaling, may be a mechanism by which integrin alpha IIbbeta 3 function is regulated.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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