Phosphorylation of dense-plaque proteins talin and paxillin during tracheal smooth muscle contraction.
Phosphorylation of dense-plaque proteins talin and paxillin during tracheal smooth muscle contraction.
复制标题
气管平滑肌收缩过程中致密斑块蛋白talin和paxillin的磷酸化。
DOI：
10.1152/ajpcell.1995.268.3.c563
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发表时间：
1995
期刊：
影响因子：
--
通讯作者：
Gunst,SJ
中科院分区：
文献类型：
--
作者：
Pavalko,FM;Adam,LP;Wu,MF;Walker,TL;Gunst,SJ
收缩刺激过程中细胞-骨-膜相互作用的重组可能有助于气道平滑肌收缩的调节。我们研究了收缩刺激对肌动蛋白-膜附着蛋白talin， vinculin和paxillin磷酸化的影响。用乙酰胆碱（ACh; 10(-3) M）刺激32p标记的犬气管平滑肌条，与静止水平0.22 mol PO4(3-)/mol talin相比，丝氨酸和/或苏氨酸残基的磷酸化迅速增加2.6倍。乙酰胆碱刺激后，帕罗西林上酪氨酸残基的磷酸化增加了大约三倍。体内标记的talin和paxillin的二维磷酸化肽图谱显示在有限的位点上磷酸化。在静息或疼痛刺激的肌肉中未检测到血管蛋白磷酸化。我们得出结论，在乙酰胆碱刺激的气管平滑肌收缩过程中，talin和paxillin的磷酸化发生，并且不同的信号通路激活了磷酸化talin的丝氨酸/苏氨酸激酶和磷酸化paxillin的酪氨酸激酶。气道平滑肌细胞的药理激活可能与可收缩细丝锚定在膜上有关。
Reorganization of cytoskeletal-membrane interactions during contractile stimulation may contribute to the regulation of airway smooth muscle contraction. We investigated the effect of contractile stimulation on the phosphorylation of the actin-membrane attachment proteins talin, vinculin, and paxillin. Stimulation of 32P-labeled canine tracheal smooth muscle strips with acetylcholine (ACh; 10(-3) M) resulted in a rapid 2.6-fold increase in phosphorylation of serine and/or threonine residues, compared with resting levels of 0.22 mol PO4(3-)/mol talin. After stimulation with ACh, phosphorylation of tyrosine residues on paxillin increased approximately threefold. Two-dimensional phosphopeptide mapping of in vivo labeled talin and paxillin indicated phosphorylation on a limited number of sites. Vinculin phosphorylation was undetectable in either resting or ACh-stimulated muscle. We conclude that phosphorylation of talin and paxillin occurs during ACh-stimulated contraction of tracheal smooth muscle and that distinct signaling pathways activate a serine/threonine kinase that phosphorylates talin and a tyrosine kinase that phosphorylates paxillin. The pharmacological activation of airway smooth muscle cells might involve the anchoring of contractile filaments to the membrane.