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The transcription factor Eyes absent is a protein tyrosine phosphatase

机译：转录因子“眼睛”缺失是一种蛋白质酪氨酸磷酸酶

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摘要

Post-translational modifications provide sensitive and flexible mechanisms to dynamically modulate protein function in response to specific signalling inputs. In the case of transcription factors, changes in phosphorylation state can influence protein stability, conformation, subcellular localization, cofactor interactions, transactivation potential and transcriptional output. Here we show that the evolutionarily conserved transcription factor Eyes absent (Eya) belongs to the phosphatase subgroup of the haloacid dehalogenase (HAD) superfamily, and propose a function for it as a non-thiol-based protein tyrosine phosphatase. Experiments performed in cultured Drosophila cells and in vitro indicate that Eyes absent has intrinsic protein tyrosine phosphatase activity and can autocatalytically dephosphorylate itself. Confirming the biological significance of this function, mutations that disrupt the phosphatase active site severely compromise the ability of Eyes absent to promote eye specification and development in Drosophila. Given the functional importance of phosphorylation-dependent modulation of transcription factor activity, this evidence for a nuclear transcriptional coactivator with intrinsic phosphatase activity suggests an unanticipated method of fine-tuning transcriptional regulation.
机译：翻译后修饰提供了灵敏而灵活的机制来响应特定信号输入动态调节蛋白质功能。就转录因子而言，磷酸化状态的变化会影响蛋白质的稳定性，构象，亚细胞定位，辅因子相互作用，反式激活潜能和转录输出。在这里，我们显示出进化保守的转录因子“无眼”（Eya）属于卤酸脱卤酶（HAD）超家族的磷酸酶亚组，并提出了其作为基于非硫醇的蛋白质酪氨酸磷酸酶的功能。在培养的果蝇细胞中和体外进行的实验表明，缺失的眼睛具有内在的蛋白质酪氨酸磷酸酶活性，并且可以自我催化去磷酸化。证实该功能的生物学意义，破坏磷酸酶活性位点的突变严重损害了缺乏果蝇以促进果蝇眼形和发育的眼睛的能力。鉴于转录因子活性的磷酸化依赖性调节的功能重要性，具有固有磷酸酶活性的核转录共激活因子的这一证据表明，微调转录调控的方法出乎意料。

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