Protein phosphatase 1 associates with the integrin alpha IIb subunit and regulates signaling

doi:10.1074/jbc.C400239200

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Papers In Press, published online ahead of print June 17, 2004
J. Biol. Chem, 10.1074/jbc.C400239200
Submitted on May 26, 2004
Revised on June 10, 2004
Accepted on June 17, 2004

Protein phosphatase 1 associates with the integrin alpha IIb subunit and regulates signaling

K. Vinod Vijayan, Yan Liu, Tong-Tong Li, and Paul F. Bray

Department of Medicine, Baylor College of Medicine, Houston, TX 77030

Corresponding Author: pbray{at}bcm.tmc.edu

Regulation of integrin activation occurs by specific interactions among cytoplasmic proteins and integrin alpha and beta cytoplasmic tails. We report that the catalytic subunit of protein phosphatase-1 (PP1c) constitutively associates with the prototypic integrin alpha IIb beta 3 in platelets and in cell lines over expressing the integrin. PP1c binds directly to the cytoplasmic domain of integrin alpha IIb subunit containing a conserved PP1c binding motif 989KVGF992. Anchored PP1c is inactive, while thrombin-induced platelet aggregation or fibrinogen-alphaIIb beta 3 engagement caused PP1c dissociation and concomitant activation as revealed by dephosphorylation of PP1c substrate, myosin light chain. Inhibition of ligand binding to activated alphaIIb beta 3 blocks PP1c dissociation and represses PP1c activation. These studies reveal a previously unrecognized role for integrins whereby the alpha subunit cytoplasmic tail localizes the machinery for initiating and temporally maintaining the regulatory signaling activity of a phosphatase.

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