Letter to the editor: "KDAC and the regulation of nonnuclear smooth muscle protein acetylation".
Letter to the editor: "KDAC and the regulation of nonnuclear smooth muscle protein acetylation".
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致编辑的信：“KDAC 和非核平滑肌蛋白乙酰化的调节”。
DOI：
10.1152/ajpcell.00208.2014
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发表时间：
2014
期刊：
影响因子：
--
通讯作者：
Taggart MJ
中科院分区：
文献类型：
--
作者：
Taggart MJ
致编辑：我们很感兴趣地阅读了李等人最近发表的论文。(4)标题为“组蛋白去乙酰化酶8调节平滑肌组织中的皮质醇去乙酰化和收缩”。非核平滑肌蛋白的乙酰化翻译后修饰是一种重要的调控机制，我们的注意力被吸引到这篇文章的几个方面。首先，作者使用泛HDAC抑制剂XXIV（如由化合物的商业来源提供的信息所示：http：//www. emdmillipore。com/GB/en/product/HDAC-Inhibitor-XXIV% 2C-OSU-HDAC-44-Calbiochem，EMD_BIO-382181？CategoryName 0000026000095 e400020023 &CategoryDomainNameMerck-MerckMillipore#锚_PDS），但声称其产生HDAC 8特定的信息。这似乎是一种过度解释，忽视了其他HDAC贡献的可能性。例如，在短发夹RNA介导的HDAC 8表达减少后，没有关于化合物有效性的任何数据。其次，对于共免疫定位实验，未提供适当的对照（例如，非免疫IgG沉淀），因此无法完全保证读者报告的相互作用具有特异性。第三，使用针对乙酰化赖氨酸残基的抗体进行报告cornein乙酰化变化的实验。因此，令人惊讶的是，作者选择只关注Coronin赖氨酸乙酰化可能随着他们的实验操作而改变的可能性。人们推测，抗体会识别许多乙酰化状态已经改变的蛋白质。第四，令人不安的是，作者没有将他们的工作放在本专题的适当背景下。大规模的蛋白质组学研究（例如，参考文献5）已经揭示了数千种蛋白质，其中许多位于细胞核外并与丝状蛋白质框架相关，是乙酰化的靶点，但这一广泛的景观并未被提及。此外，不是所有的，当然，但许多方面的研究李等人。(4)关于HDAC 8在介导非核、细胞骨架蛋白乙酰化以及由此产生的平滑肌力中可能具有的潜在作用，与先前在血管和非血管平滑肌中报道的工作相似（1，2，3）。然而Li等人(4)没有提到这些文件。在此背景下，我们（1）先前报道了1）HDAC 8抑制剂化合物2和泛HDAC抑制剂曲马斯他汀A的平滑肌松弛作用; 2）HDAC 8与包括皮质激素在内的几种平滑肌丝状蛋白的共免疫沉淀;和3）在HDAC 8抑制后，包括皮质激素在内的几种平滑肌丝状蛋白的乙酰化形式的免疫沉淀增加。事实上，在平滑肌和其他组织中，许多非核蛋白质是乙酰化的靶点，我们将脱乙酰酶称为KDAC（赖氨酸脱乙酰酶），而不是HDAC（1）。这似乎与KDAC 8特别相关。总之，我们欢迎Li等人的贡献。(4)本文的主要目的是讨论KDAC修饰平滑肌蛋白的问题，但同时也表明，不应忽视这篇文章的大部分优点是为关于这一主题的现有工作增加信息。
TO THE EDITOR: We were intrigued to read the paper recently published by Li et al.(4) entitled “Histone deacetylase 8 regulates cortactin deacetylation and contraction in smooth muscle tissues.” The posttranslational modification of nonnuclear smooth muscle proteins by acetylation is emerging as an important regulatory mechanism, and our attention was drawn to several aspects of the article. First, the authors used the pan-HDAC inhibitor XXIV (as indicated by information provided by the commercial source of the compound: http://www. emdmillipore. com/GB/en/product/HDAC-Inhibitor-XXIV% 2C-OSU-HDAC-44—Calbiochem, EMD_BIO-382181? CategoryName00000026000095e400020023 &CategoryDomainNameMerck-MerckMillipore# anchor_PDS), yet claimed it to yield information specific to HDAC8. This seemed to be an overinterpretation and ignored the possibility of a contribution from other HDACs. There was not, for example, any data on the effectiveness of the compound after short hairpin RNA-mediated reduction of HDAC8 expression. Second, for the coimmunolocalization experiments the appropriate controls (eg, nonimmune IgG precipitations) were not presented, thus denying the reader complete security that the reported interactions were specific. Third, the experiments reporting changes in cortactin acetylation were performed using an antibody directed against acetylated lysine residues. It is therefore surprising that the authors chose to focus on only the possibility that cortactin lysine acetylation may have changed with their experimental manoeuvers. The antibody, one presumes, will have picked up many proteins whose acetylation status will have been altered. Fourth, it is disconcerting that the authors failed to place their work in an appropriate context of the topic. Large-scale proteomic studies (eg, Ref. 5) have revealed several thousand proteins, many resident outwith the nucleus and related to filamentous protein frameworks, to be targets for acetylation, yet this broad landscape was not mentioned. In addition, not all, of course, but many aspects of the study by Li et al.(4) with respect to the potential role that HDAC8 may have in mediating nonnuclear, cytoskeletal protein acetylation and, thereby, smooth muscle force production were similar to work reported previously in vascular and nonvascular smooth muscle (1, 2, 3). Yet Li et al.(4) made no reference to these papers. In this context we (1) previously reported 1) the smooth muscle relaxatory actions of the HDAC8 inhibitor compound 2 and the pan-HDAC inhibitor trichostatin A; 2) the coimmunoprecipitation of HDAC8 with several smooth muscle filamentous proteins including cortactin; and 3) the increased immunoprecipitation of acetylated forms of several smooth muscle filamentous proteins, including cortactin, following HDAC8 inhibition. Indeed, in appreciation of the burgeoning data suggestive of many nonnuclear proteins being targets of acetylation, in smooth muscle and other tissues, we referred to deacetylases as KDACs (for lysine deacetylase) rather than HDACs (1). This seems particularly pertinent for KDAC8. In summary, we welcome the contributions of Li et al.(4) to the topic of smooth muscle protein modification by KDACs, yet suggest it should not go unnoticed that much of the merit of this article is to add information to an already existing body of work on this topic.
影响因子：
5.5
作者：
Li, Jia;Chen, Shu;Tang, Dale D.
通讯作者：
Tang, Dale D.