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  • A role for the tyrosine kinase Pyk2 in depolarization-induced contraction of vascular smooth muscle.

A role for the tyrosine kinase Pyk2 in depolarization-induced contraction of vascular smooth muscle.

The Journal of biological chemistry (2015-02-26)
Ryan D Mills, Mitsuo Mita, Jun-ichi Nakagawa, Masaru Shoji, Cindy Sutherland, Michael P Walsh
ABSTRACT

Depolarization of the vascular smooth muscle cell membrane evokes a rapid (phasic) contractile response followed by a sustained (tonic) contraction. We showed previously that the sustained contraction involves genistein-sensitive tyrosine phosphorylation upstream of the RhoA/Rho-associated kinase (ROK) pathway leading to phosphorylation of MYPT1 (the myosin-targeting subunit of myosin light chain phosphatase (MLCP)) and myosin regulatory light chains (LC20). In this study, we addressed the hypothesis that membrane depolarization elicits activation of the Ca(2+)-dependent tyrosine kinase Pyk2 (proline-rich tyrosine kinase 2). Pyk2 was identified as the major tyrosine-phosphorylated protein in response to membrane depolarization. The tonic phase of K(+)-induced contraction was inhibited by the Pyk2 inhibitor sodium salicylate, which abolished the sustained elevation of LC20 phosphorylation. Membrane depolarization induced autophosphorylation (activation) of Pyk2 with a time course that correlated with the sustained contractile response. The Pyk2/focal adhesion kinase (FAK) inhibitor PF-431396 inhibited both phasic and tonic components of the contractile response to K(+), Pyk2 autophosphorylation, and LC20 phosphorylation but had no effect on the calyculin A (MLCP inhibitor)-induced contraction. Ionomycin, in the presence of extracellular Ca(2+), elicited a slow, sustained contraction and Pyk2 autophosphorylation, which were blocked by pre-treatment with PF-431396. Furthermore, the Ca(2+) channel blocker nifedipine inhibited peak and sustained K(+)-induced force and Pyk2 autophosphorylation. Inhibition of Pyk2 abolished the K(+)-induced translocation of RhoA to the particulate fraction and the phosphorylation of MYPT1 at Thr-697 and Thr-855. We conclude that depolarization-induced entry of Ca(2+) activates Pyk2 upstream of the RhoA/ROK pathway, leading to MYPT1 phosphorylation and MLCP inhibition. The resulting sustained elevation of LC20 phosphorylation then accounts for the tonic contractile response to membrane depolarization.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Phosphotyrosine Antibody, clone 4G10®, clone 4G10®, Upstate®, from mouse
Sigma-Aldrich
ROKα/ROCK-II Protein, active, rat, 10 µg, Active, rat, N-terminal, His-tagged, fusion protein corresponding to amino acids 2-543 of rat ROKa/ROCK-II. For use in Kinase Assays.
Sigma-Aldrich
Anti-phospho-MYPT1 (Thr850) Antibody, Upstate®, from rabbit
Sigma-Aldrich
Anti-phospho-MYPT1 (Thr696) Antibody, from rabbit, purified by affinity chromatography