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首页> 外文期刊>Cellular immunology >TAK1 lessens the activity of the paracaspase MALT1 during T cell receptor signaling
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TAK1 lessens the activity of the paracaspase MALT1 during T cell receptor signaling

机译：Tak1减少了在T细胞受体信号传导期间的帕拉克酶Malt1的活性

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摘要

The CARMAl-BCL10-MALT1 (CBM) complex couples antigen receptors to the activation of Nuclear Factor kappa B (NF-kappa B) transcription factors in T/B lymphocytes. Within this signalosome, the MALT1 paracaspase serves dual roles: it is a crucial adaptor for signal transduction to NF-kappa B signaling, and a protease that shapes NF-kappa B activity and lymphocyte activation. Although a subtle choreography of ubiquitination and phosphorylation orchestrate the CBM, how precisely this complex and MALT1 enzyme are regulated continue to be elucidated. Here, we report that the chemical inhibition or the siRNA-based silencing of transforming growth factor beta-activated kinase 1 (TAK1), a known partner of the CBM complex required for NF-kappa B activation, enhanced the processing of MALT1 substrates. We further show that the assembly of the CBM as well as the ubiquitination of MALT1 was augmented when TAK1 was inhibited. Thus, TAK1 may initiate a negative feedback loop to finely tune the CBM complex activity.
机译：CARMAl-BCL10-MALT1（CBM）复合物将抗原受体与T/B淋巴细胞中核因子-κB（NF-κB）转录因子的激活偶联。在这个信号体中，MALT1半胱天冬酶具有双重作用：它是NF-κB信号转导的关键适配器，也是一种塑造NF-κB活性和淋巴细胞活化的蛋白酶。尽管泛素化和磷酸化的微妙编排协调了CBM，但这种复合物和MALT1酶的精确调节仍有待阐明。在这里，我们报告了转化生长因子β激活激酶1（TAK1）的化学抑制或基于siRNA的沉默，TAK1是NF-κB激活所需的CBM复合物的已知伙伴，增强了MALT1底物的加工。我们进一步表明，当TAK1被抑制时，CBM的组装以及MALT1的泛素化增强。因此，TAK1可启动负反馈回路，以微调CBM复杂活动。

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