TRPV4/6通道钙调素结合域的突变赋予结肠腺癌细胞侵袭性。

Atousa Arbabian, Mircea Iftinca, Christophe Altier, Param Priya Singh, Hervé Isambert, Sylvie Coscoy
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引用次数: 11

摘要

瞬时受体电位(TRP)通道是由热、机械或化学刺激门控的多模态阳离子通道家族,其中许多通道参与细胞增殖、凋亡或细胞周期的控制。从进化的角度来看,TRP家族的特点是复制基因的高度保守性,起源于脊椎动物的全基因组复制。从理论上讲,这种“同源”基因的保存与基因突变时产生对生物体有害的表型的可能性增加有关。我们的目的是通过实验验证TRP突变,特别是功能获得,可能与癌症中有害表型的产生有关,例如侵袭性获得。事实上,许多TRP通道与癌症进展有关,并在各种类型的癌症中表现出表达水平的变化。然而,TRP突变在癌症中的记录很少。我们以TRPV家族的2个成员TRPV4和TRPV6为研究对象,研究了功能获得性突变对侵袭性的影响。TRPV通道具有c端钙调素结合域(CaMBD),该域对调节蛋白质功能具有重要作用,其机制取决于通道(通道失活/增强、细胞骨架调节)。我们研究了TRPV4和TRPV6 cambd中模拟组成磷酸化的突变的影响:TRPV4 S823D, S824D和T813D, TRPV6 S691D, S692D和T702。我们发现,大多数这些突变体诱导TRPV4和TRPV6对结肠腺癌SW480细胞的侵袭性增强。虽然TRPV6 S692D和T702D突变体的入侵增加与突变体通道活性增加相关,但TRPV4突变体的情况并非如此,这表明不同的机制具有相同的有害表型增益的全局效应。这凸显了寻找与癌症有关的TRP突变的潜在重要性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

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Mutations in calmodulin-binding domains of TRPV4/6 channels confer invasive properties to colon adenocarcinoma cells.

Transient receptor potential (TRP) channels form a family of polymodal cation channels gated by thermal, mechanical, or chemical stimuli, with many of them involved in the control of proliferation, apoptosis, or cell cycle. From an evolutionary point of view, TRP family is characterized by high conservation of duplicated genes originating from whole-genome duplication at the onset of vertebrates. The conservation of such "ohnolog" genes is theoretically linked to an increased probability of generating phenotypes deleterious for the organism upon gene mutation. We aimed to test experimentally the hypothesis that TRP mutations, in particular gain-of-function, could be involved in the generation of deleterious phenotypes involved in cancer, such as gain of invasiveness. Indeed, a number of TRP channels have been linked to cancer progression, and exhibit changes in expression levels in various types of cancers. However, TRP mutations in cancer have been poorly documented. We focused on 2 TRPV family members, TRPV4 and TRPV6, and studied the effect of putative gain-of-function mutations on invasiveness properties. TRPV channels have a C-terminal calmodulin-binding domain (CaMBD) that has important functions for regulating protein function, through different mechanisms depending on the channel (channel inactivation/potentiation, cytoskeleton regulation). We studied the effect of mutations mimicking constitutive phosphorylation in TRPV4 and TRPV6 CaMBDs: TRPV4 S823D, S824D and T813D, TRPV6 S691D, S692D and T702. We found that most of these mutants induced a strong gain of invasiveness of colon adenocarcinoma SW480 cells, both for TRPV4 and TRPV6. While increased invasion with TRPV6 S692D and T702D mutants was correlated to increased mutant channel activity, it was not the case for TRPV4 mutants, suggesting different mechanisms with the same global effect of gain in deleterious phenotype. This highlights the potential importance to search for TRP mutations involved in cancer.

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