Myosin light chain kinase A is activated by cGMP-dependent and cGMP-independent pathways
Myosin light chain kinase A is activated by cGMP-dependent and cGMP-independent pathways
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DOI：
10.1016/j.febslet.2006.03.008
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发表时间：
2006-04-03
期刊：
影响因子：
3.5
通讯作者：
Smith, JL
中科院分区：
文献类型：
--
作者：
Goldberg, JM;Wolpin, ES;Smith, JL
用化学引诱物cAMP刺激网骨藻细胞导致肌球蛋白调节轻链（RLC）的瞬时磷酸化。我们发现，肌球蛋白轻链激酶A（MLCK-A）是负责RLC磷酸化在趋化过程中，MLCK-A本身是瞬时磷酸化的苏氨酸-166，显着增加其催化活性。MLCK-A在趋化过程中的活化对细胞cGMP水平和cGMP结合蛋白GbpC高度响应。MLCK-A（-）细胞具有部分胞质分裂缺陷，并且不响应于伴刀豆球蛋白A（conA）而磷酸化RLC，但是缺乏cGMP或GbpC的细胞正常分裂并且响应于conA而磷酸化。因此，MLCK-A被胞质分裂过程中激活的cGMP/GbpC非依赖性机制或conA激活，以及趋化过程中的cGMP/GbpC依赖性途径激活。(c)2006年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Stimulation of Dictyostelium cells with the chemoattractant cAMP results in transient phosphorylation of the myosin regulatory light chain (RLC). We show that myosin light chain kinase A (MLCK-A) is responsible for RLC phosphorylation during chemotaxis, and that MLCK-A itself is transiently phosphorylated on threonine-166, dramatically increasing its catalytic activity. MLCK-A activation during chemotaxis is highly responsive to cellular cGMP levels and the cGMP-binding protein GbpC. MLCK-A(-) cells have a partial cytokinesis defect, and do not phosphorylate RLC in response to concanavalin A (conA), but cells lacking cGMP or GbpC divide normally and phosphorylate in response to conA. Thus MLCK-A is activated by a cGMP/GbpC-independent mechanism activated during cytokinesis or by conA, and a cGMP/GbpC-dependent pathway during chemotaxis. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.