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The teneurin C-terminal domain possesses nuclease activity and is apoptogenic

机译:Teneurin C末端结构域具有核酸酶活性,并具有凋亡作用

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Teneurins are type 2 transmembrane proteins expressed by developing neurons during periods of synaptogenesis and apoptosis. Neurons expressing teneurin-1 synapse with other teneurin-1-expressing neurons, and neurons expressing teneurin-2 synapse with other teneurin-2-expressing neurons. Knockdowns and mutations of teneurins lead to abnormal neuronal connections, but the mechanisms underlying teneurin action remain unknown. Teneurins appear to have evolved via horizontal gene transfer from prokaryotic proteins involved in bacterial self-recognition. The bacterial teneurin-like proteins contain a cytotoxic C-terminal domain that is encapsulated in a tyrosine-aspartic acid repeat barrel. Teneurins are likely to be organized in the same way, but it is unclear if the C-terminal domains of teneurins have cytotoxic properties. Here we show that expression of teneurin C-terminal domains or the addition of purified teneurin C-terminal domains leads to an increase in apoptosisin vitro. The C-terminal domains of teneurins are most similar to bacterial nucleases, and purified C-terminal domains of teneurins linearize pcDNA3 and hydrolyze mitochondrial DNA. We hypothesize that yet to be identified stimuli lead to the release of the encapsulated teneurin C-terminal domain into the intersynaptic region, resulting in programmed cell death or the disruption of mitochondrial DNA and the subsequent pruning of inappropriate contacts.
机译:Teneurins是2型跨膜蛋白,在突触形成和凋亡期间由发育中的神经元表达。表达Teneurin-1突触的神经元与其他表达Teneurin-1的神经元,以及表达Teneurin-2突触的神经元与其他表达Teneurin-2的神经元。敲低腱蛋白的突变和突变会导致异常的神经元连接,但腱蛋白作用的潜在机制尚不清楚。 Teneurins似乎是通过水平基因转移从参与细菌自我识别的原核蛋白进化而来的。细菌腱蛋白样蛋白包含细胞毒性的C末端结构域,该结构域封装在酪氨酸-天冬氨酸重复桶中。 Teneurins可能以相同的方式组织,但尚不清楚Teneurins的C末端结构域是否具有细胞毒性。在这里,我们表明腱蛋白C末端域的表达或纯化的腱蛋白C末端域的添加导致体外凋亡的增加。 Teneurins的C末端结构域与细菌核酸酶最为相似,纯化的Teneurins的C末端结构域使pcDNA3线性化并水解线粒体DNA。我们假设尚未确定的刺激导致封装的Teneurin C末端域释放到突触间区域,导致程序性细胞死亡或线粒体DNA破坏和随后的不适当接触修剪。

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