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Direct Interaction between Anthrax Toxin Receptor 1 and the Actin Cytoskeleton

机译:炭疽毒素受体1和肌动蛋白细胞骨架之间的直接相互作用。

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摘要

The protective antigen component of anthrax toxin binds the I domain of the anthrax toxin receptors, ANTXR1 and ANTXR2, in a manner akin to how integrins bind their ligands. The I domains of integrins and ANTXR1 both have high- and low-affinity conformations, and the cytosolic tails of these receptors associate with the actin cytoskeleton. The association of ANTXR1 with the cytoskeleton correlates with weakened binding to PA, although a mechanistic explanation for this observation is lacking. Here, we identified a segment in the cytoplasmic tail of ANTXR1 required for its association with the cytoskeleton. We synthesized a 60-mer peptide based on this segment and demonstrated a direct interaction between the peptide and β-actin, indicating that in contrast to integrins, ANTXR1 does not use an adaptor to bind the cytoskeleton. This peptide orders actin filaments into arrays, demonstrating an actin bundling activity that is novel for a membrane protein
机译:炭疽毒素的保护性抗原成分以类似于整联蛋白如何结合其配体的方式结合炭疽毒素受体的I结构域ANTXR1和ANTXR2。整联蛋白和ANTXR1的I结构域均具有高亲和力和低亲和力构象,并且这些受体的胞质尾与肌动蛋白的细胞骨架相关。 ANTXR1与细胞骨架的关联与与PA的结合减弱有关,尽管缺乏对此现象的机械解释。在这里,我们确定了ANTXR1在细胞质尾巴中的一个片段,该片段需要与细胞骨架关联。我们基于该片段合成了60个肽段,并证明了该肽段与β-肌动蛋白之间存在直接相互作用,这表明与整联蛋白相比,ANTXR1不使用衔接子来结合细胞骨架。该肽将肌动蛋白丝排列成阵列,证明了膜蛋白的新型肌动蛋白捆绑活性

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  • 来源
    《Biochemistry》 |2009年第44期|p.10577-10581|共5页
  • 作者单位

    Kristopher M. Garlick and Jeremy Mogridge*Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto, Ontario M5S 1A8, Canada;

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