Mills Ryan D, Mita Mitsuo, Nakagawa Jun-ichi, Shoji Masaru, Sutherland Cindy, Walsh Michael P
From the Smooth Muscle Research Group, Department of Biochemistry and Molecular Biology, Libin Cardiovascular Institute and Hotchkiss Brain Institute, University of Calgary, Calgary, Alberta T2N 4N1, Canada and.
the Department of Pharmacodynamics, Meiji Pharmaceutical University, 2-522-1 Noshio, Kiyose, Tokyo 204-8588, Japan.
J Biol Chem. 2015 Apr 3;290(14):8677-92. doi: 10.1074/jbc.M114.633107. Epub 2015 Feb 24.
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.
血管平滑肌细胞膜的去极化引发快速(相性)收缩反应,随后是持续(紧张性)收缩。我们之前表明,持续收缩涉及RhoA/ Rho相关激酶(ROK)途径上游的染料木黄酮敏感的酪氨酸磷酸化,导致MYPT1(肌球蛋白轻链磷酸酶(MLCP)的肌球蛋白靶向亚基)和肌球蛋白调节轻链(LC20)的磷酸化。在本研究中,我们探讨了膜去极化引发Ca(2+)依赖性酪氨酸激酶Pyk2(富含脯氨酸的酪氨酸激酶2)激活的假说。Pyk2被确定为响应膜去极化的主要酪氨酸磷酸化蛋白。K(+)诱导收缩的紧张相被Pyk2抑制剂水杨酸钠抑制,水杨酸钠消除了LC20磷酸化的持续升高。膜去极化诱导Pyk2的自磷酸化(激活),其时程与持续收缩反应相关。Pyk2/粘着斑激酶(FAK)抑制剂PF-431396抑制对K(+)收缩反应的相性和紧张性成分、Pyk2自磷酸化以及LC20磷酸化,但对calyculin A(MLCP抑制剂)诱导的收缩无影响。在细胞外Ca(2+)存在下,离子霉素引发缓慢、持续的收缩和Pyk2自磷酸化,这被PF-431396预处理所阻断。此外,Ca(2+)通道阻滞剂硝苯地平抑制K(+)诱导的峰值和持续力以及Pyk2自磷酸化。抑制Pyk2消除了K(+)诱导的RhoA向颗粒部分的转位以及MYPT1在Thr-697和Thr-855的磷酸化。我们得出结论,去极化诱导的Ca(2+)内流在RhoA/ROK途径上游激活Pyk2,导致MYPT1磷酸化和MLCP抑制。由此产生的LC20磷酸化的持续升高随后解释了对膜去极化的紧张性收缩反应。