The juxtamembrane domain of the E-cadherin cytoplasmic tail contributes to its interaction with Myosin VI.

Bioarchitecture Pub Date : 2012-09-01 DOI:10.4161/bioa.22082
Sabine Mangold, Suzanne J Norwood, Alpha S Yap, Brett M Collins
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引用次数: 12

Abstract

We recently identified the atypical myosin, Myosin VI, as a component of epithelial cell-cell junctions that interacts with E-cadherin. Recombinant proteins bearing the cargo-binding domain of Myosin VI (Myo VI-CBD) or the cytoplasmic tail of E-cadherin can interact directly with one another. In this report we further investigate the molecular requirements of the interaction between Myo VI-CBD and E-cadherin combining truncation mutation analysis with in vitro binding assays. We report that a short (28 amino acid) juxtamembrane region of the cadherin cytoplasmic tail is sufficient to bind Myo VI-CBD. However, central regions of the cadherin tail adjacent to the juxtamembrane sequence also display binding activity for Myo VI-CBD. It is therefore possible that the cadherin tail bears two binding sites for Myosin VI, or an extended binding site that includes the juxtamembrane region. Nevertheless, our biochemical data highlight the capacity for the juxtamembrane region to interact with functionally-significant cytoplasmic proteins.

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e -钙粘蛋白细胞质尾部的近膜结构域有助于其与肌球蛋白VI的相互作用。
我们最近发现了非典型肌凝蛋白,肌凝蛋白VI,作为上皮细胞-细胞连接的一个组成部分,与e -钙粘蛋白相互作用。重组蛋白携带Myosin VI (Myo VI- cbd)的货物结合域或E-cadherin的细胞质尾部可以直接相互作用。在本报告中,我们结合截断突变分析和体外结合分析进一步研究了Myo VI-CBD与E-cadherin相互作用的分子要求。我们报道了钙粘蛋白细胞质尾部的短(28个氨基酸)近膜区域足以结合Myo VI-CBD。然而,钙粘蛋白尾部靠近近膜序列的中心区域也显示出对Myo VI-CBD的结合活性。因此,钙粘蛋白尾部可能具有肌凝蛋白VI的两个结合位点,或者包含近膜区域的延伸结合位点。然而,我们的生化数据强调了近膜区域与功能显著的细胞质蛋白相互作用的能力。
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