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首页> 外文期刊>American Journal of Physiology >Abl activation regulates the dissociation of CAS from cytoskeletal vimentin by modulating CAS phosphorylation in smooth muscle
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Abl activation regulates the dissociation of CAS from cytoskeletal vimentin by modulating CAS phosphorylation in smooth muscle

机译：Abl激活通过调节平滑肌中的CAS磷酸化来调节CAS与细胞骨架波形蛋白的解离

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摘要

Abl is a nonreceptor tyrosine kinase that is required for smooth muscle contraction. However, the mechanism by which Abl regulates smooth muscle contraction is not completely understood. In the present study, Abl underwent phosphorylation at Tyr412 (an index of Abl activation) in smooth muscle in response to contractile activation. Treatment with a cell-permeable decoy peptide, but not the control peptide, attenuated Abl phosphorylation during contractile stimulation. Treatment with the decoy peptide did not affect the association of Abl with the cytoskeletal protein vinculin and the spatial location of vinculin in smooth muscle. Inhibition of Abl phosphorylation by the decoy peptide attenuated the agonist-induced phosphorylation of Crk-associated substrate (CAS), an adapter protein participating in the signaling processes that regulate force development in smooth muscle. Additionally, previous studies have shown that contractile stimulation triggers the dissociation of CAS from the vimentin network, which is important for cytoskeletal signaling and contraction in smooth muscle. In this report, the decrease in the amount of CAS in cytoskeletal vimentin in response to contractile activation was reversed by the Abl inhibition with the decoy peptide. Moreover, force development and the enhancement of F-actin-to-G-actin ratios (an indication of actin polymerization) upon contractile activation were also attenuated by the Abl inhibition. However, myosin phosphorylation induced by contractile activation was not affected by the inhibition of Abl. These results suggest that Abl regulates the dissociation of CAS from the vimentin network, actin polymerization, and contraction by modulating CAS phosphorylation in smooth muscle.
机译：Abl是平滑肌收缩所需的非受体酪氨酸激酶。但是，Abl调节平滑肌收缩的机制尚不完全清楚。在本研究中，响应于收缩激活，Abl在平滑肌的Tyr412处进行磷酸化（Abl激活的指标）。用细胞可渗透的诱饵肽而不是对照肽进行的处理在收缩刺激过程中减弱了Abl磷酸化。诱饵肽治疗不会影响Abl与细胞骨架蛋白纽蛋白的结合以及纽蛋白在平滑肌中的空间位置。诱饵肽对Abl磷酸化的抑制作用减弱了激动剂诱导的Crk相关底物（CAS）的磷酸化，该底物是参与调节平滑肌力发展的信号传导过程的衔接蛋白。此外，以前的研究表明，收缩刺激会触发CAS从波形蛋白网络中解离，这对于平滑肌中细胞骨架的信号传导和收缩非常重要。在此报告中，诱变肽对Abl的抑制作用可以逆转收缩激活引起的细胞骨架波形蛋白中CAS数量的减少。此外，通过Abl抑制还减弱了力激活和在收缩活化时F-肌动蛋白与G-肌动蛋白之比的增加（肌动蛋白聚合的指示）。然而，由收缩活化诱导的肌球蛋白磷酸化不受Abl的抑制作用。这些结果表明，Abl通过调节平滑肌中的CAS磷酸化来调节CAS从波形蛋白网络的解离，肌动蛋白的聚合和收缩。

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