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TRAF2-mediated Lys63-linked ubiquitination of DUSP14/MKP6 is essential for its phosphatase activity

机译：TRAF2介导的DUSP14 / MKP6的Lys63连接的泛素化对其磷酸酶活性至关重要

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摘要

Dual-specificity phosphatase 14 (DUSP14, also known as MKP6) is a MAP kinase phosphatase that dephosphorylates JNK, ERK, and p38 in vitro. We recently reported that DUSP14 negatively regulates T-cell activation and immune responses by interfering activation of TAB1-TAK1 complex. However, the molecular mechanism that regulates the phosphatase activity of DUSP14 remains unclear. Here, we report the post-translational modification of DUSP14 by ubiquitination. Mass spectrometry and mutational analyses identified that DUSP14 was Lys63linked ubiquitinated at lysine 103 residue. Furthermore, DUSP14 inducibly interacted with the E3 ligase TRAF2 during T-cell receptor (TCR) signaling; TRAF2 shRNA knockdown reduced the DUSP14 ubiquitination. We also show that ubiquitination of DUSP14 was required for its phosphatase activity during TCR signaling. Together, these findings reveal a novel mechanism by which TRAF2 mediates Lys63-linked ubiquitination of DUSP14, leading to DUSP14 activation in T cells. (C) 2015 Elsevier Inc All rights reserved.
机译：双特异性磷酸酶14（DUSP14，也称为MKP6）是MAP激酶磷酸酶，可在体外使JNK，ERK和p38脱磷酸。我们最近报道，DUSP14通过干扰TAB1-TAK1复合物的活化来负调控T细胞活化和免疫反应。但是，尚不清楚调节DUSP14磷酸酶活性的分子机制。在这里，我们报道了泛素化对DUSP14的翻译后修饰。质谱和突变分析确定DUSP14在赖氨酸103残基处被Lys63连接泛素化。此外，DUSP14在T细胞受体（TCR）信号传导过程中可诱导地与E3连接酶TRAF2相互作用。 TRAF2 shRNA敲低可降低DUSP14泛素化。我们还显示DUSP14的泛素化是TCR信号传导期间其磷酸酶活性所必需的。在一起，这些发现揭示了TRAF2介导DUSP14的Lys63连锁泛素化的新机制，从而导致DUSP14在T细胞中的活化。 （C）2015 Elsevier Inc保留所有权利。

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