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首页> 外文期刊>Biochemistry >Kinetic Analysis Reveals Differences in the Binding Mechanism of Calmodulin and Calmodulin-like Protein to the IQ Motifs of Myosin-10
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Kinetic Analysis Reveals Differences in the Binding Mechanism of Calmodulin and Calmodulin-like Protein to the IQ Motifs of Myosin-10

机译：动力学分析揭示了钙调蛋白和钙调蛋白样蛋白与肌球蛋白10智商基元的结合机制的差异。

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摘要

Myo10 is an unconventional myosin with important functions in filopodial motility, cell migra-ntion, and cell adhesion. The neck region ofMyo10 contains three IQmotifs that bind calmodulin (CaM) or thentissue-restricted calmodulin-like protein (CLP) as light chains. However, little is known about themechanismnof light chain binding to the IQ motifs inMyo10. Binding of CaMand CLP to each IQ motif was assessed bynnondenaturing gel electrophoresis and by stopped-flow experiments using fluorescence-labeled CaM andnCLP. Although the binding kinetics are different in each case, there are similarities in the mechanism ofnbinding of CaMand CLP to IQ1 and IQ2: for both IQ motifs Ca2þ increased the binding affinity, mainly bynincreasing the rate of the forward steps. The general kineticmechanismcomprises a two-step process, which innsome casesmay involve the binding of a second IQmotif with lower affinity. For IQ3, however, the kinetics ofnCaM binding is very different from that of CLP. In both cases, binding in the absence of Ca2þ is poor, andnaddition of Ca2þ decreases the Kd to below 10 nM.However, while the CaMbinding kinetics are complex andnbest fitted by a multistep model, binding of CLP is fitted by a relatively simple two-step model. The resultsnshow that, in keeping with growing structural evidence, complexes between CaM or CaM-like myosin lightnchains and IQ motifs are highly diverse and depend on the specific sequence of the particular IQ motif as wellnas the light chain.
机译：Myo10是一种非常规的肌球蛋白，在丝状运动，细胞迁移和细胞粘附方面具有重要功能。 Myo10的颈部区域包含三个结合钙调蛋白（CaM）或受组织限制的钙调蛋白样蛋白（CLP）作为轻链的IQmotif。然而，关于Myo10中的轻链与IQ基序结合的机理尚不清楚。通过非变性凝胶电泳和使用荧光标记的CaM和nCLP的停流实验评估CaMand CLP与每个IQ基序的结合。尽管在每种情况下结合动力学都不同，但是CaM和CLP结合IQ1和IQ2的机理相似：对于两个IQ基序，Ca2 +均增加了结合亲和力，主要是通过增加前进步骤的速率。一般的动力学机制包括两步过程，在某些情况下可能涉及以较低亲和力结合第二个IQmotif。但是，对于IQ3，nCaM结合的动力学与CLP的动力学有很大不同。在这两种情况下，缺乏Ca2 +的结合都很差，添加Ca2 +会使Kd降至10 nM以下。然而，尽管CaM结合动力学很复杂，并且最好用多步模型拟合，但CLP的结合是通过相对简单的两步拟合：步模型。结果表明，与不断增长的结构证据相一致，CaM或类似CaM的肌球蛋白轻链与IQ基序之间的复合物高度多样化，并取决于特定IQ基序的特定序列以及轻链。

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  • 来源
    《Biochemistry》 |2010年第37期|p.8105-8116|共12页
  • 作者

    Ariel J. Caride Richard D. Bennett and Emanuel E. Strehler;

  • 作者单位

    Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, Minnesota 55905‡Present address: McLaughlin Research Institute, Great Falls, MT 59405.;

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