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首页> 外文期刊>Nature immunology >The protease activity of the paracaspase MALT1 is controlled by monoubiquitination
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The protease activity of the paracaspase MALT1 is controlled by monoubiquitination

机译：半胱天冬酶MALT1的蛋白酶活性受单泛素化作用的控制

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摘要

The protease activity of the paracaspase MALT1 is central to lymphocyte activation and lymphomagenesis, but how this activity is controlled remains unknown. Here we identify a monoubiquitination of MALT1 on Lys644 that activated the protease function of MALT1. Monoubiquitinated MALT1 had enhanced protease activity, whereas a ubiquitination-deficient MALT1 mutant with replacement of that lysine with arginine (MALT1(K644R)) had less protease activity, which correlated with impaired induction of interleukin 2 (IL-2) via the T cell antigen receptor in activated T cells. Expression of MALT1(K644R) diminished the survival of cells derived from diffuse large B cell lymphoma of the activated B cell-like subtype (ABC DLBCL), which require constitutive protease activity of MALT1 for survival. Thus, monoubiquitination of MALT1 is essential for its catalytic activation and is therefore a potential target for the treatment of ABC-DLBCL and for immunomodulation. ? 2013 Nature America, Inc. All rights reserved.
机译：对半胱天冬酶MALT1的蛋白酶活性是淋巴细胞活化和淋巴瘤发生的关键，但是如何控制该活性仍然未知。在这里，我们确定Lys644上MALT1的单泛素化激活了MALT1的蛋白酶功能。单泛素化的MALT1具有增强的蛋白酶活性，而用精氨酸（MALT1（K644R））取代赖氨酸的泛素化缺陷的MALT1突变体具有较小的蛋白酶活性，这与通过T细胞抗原诱导的白介素2（IL-2）的诱导受损有关。激活的T细胞中的受体MALT1（K644R）的表达减少了活化的B细胞样亚型（ABC DLBCL）的弥漫性大B细胞淋巴瘤衍生的细胞的存活，该细胞需要MALT1的组成型蛋白酶活性才能存活。因此，MALT1的单泛素化对其催化激活至关重要，因此是治疗ABC-DLBCL和进行免疫调节的潜在靶标。 ？ 2013 Nature America，Inc.保留所有权利。

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