14-3-3β isoform is specifically acetylated at Lys51 during differentiation to the osteogenic lineage,Journal of Cellular Biochemistry

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14-3-3β isoform is specifically acetylated at Lys51 during differentiation to the osteogenic lineage
Journal of Cellular Biochemistry ( IF 3.0 ) Pub Date : 2021-08-11 , DOI: 10.1002/jcb.30128
Yesica R Frontini-López ₁ , Aldana D Gojanovich _{1,

2} , Samanta Del Veliz ₁ , Marina Uhart ₁ , Diego M Bustos _{1,

3}

Affiliation

The 14-3-3 protein family binds and regulates hundreds of serine/threonine phosphorylated proteins as an essential component of many signaling networks. Specific biological functions are currently been discovered for each of its seven isoforms in mammals. These proteins have been traditionally considered unregulated; however, its acetylation in an essential lysine residue, causing its inactivation, was recently published. Here, we studied the acetylation state of this lysine 49/51 during the osteogenic differentiation of human adipose-derived stem cells. We found that during this process, the levels of 14-3-3β (but not its isoform 14-3-3γ) acK49/51 increase, representing the first report linking this PTM to a specific isoform and a cellular process. Our results suggested that this posttranslational modification could be catalyzed by the HBO1 acetyltransferase, as overexpression of HBO1 increased specifically 14-3-3 acK49/51 acetylation. Acetylated 14-3-3 proteins are located primarily in the nucleus, where their active state has been described to bind H3 histones and many transcription factors. The inhibition of the expression of different isoforms showed that the specific silencing of the 14-3-3β gene, but not γ, increased significantly the osteogenic potential of the cells. This result correlated to the increase in acetylation of 14-3- 3β Lys 49/51 during osteogenesis. The possible role of this PTM in osteogenesis is discussed.

中文翻译：

14-3-3β 同种型在向成骨谱系分化期间在 Lys51 处特异性乙酰化

14-3-3 蛋白家族结合并调节数百种丝氨酸/苏氨酸磷酸化蛋白，作为许多信号网络的重要组成部分。目前在哺乳动物中发现了其七种同种型中的每一种的特定生物学功能。这些蛋白质传统上被认为是不受监管的。然而，最近发表了其在必需赖氨酸残基中的乙酰化，导致其失活。在这里，我们研究了人类脂肪干细胞成骨分化过程中这种赖氨酸 49/51 的乙酰化状态。我们发现在此过程中，14-3-3β（但不是其同种型 14-3-3γ）acK49/51 的水平增加，这是第一个将这种 PTM 与特定同种型和细胞过程联系起来的报告。我们的结果表明，这种翻译后修饰可以由 HBO1 乙酰转移酶催化，因为 HBO1 的过表达特异性增加了 14-3-3 acK49/51 乙酰化。乙酰化 14-3-3 蛋白主要位于细胞核中，其活性状态已被描述为结合 H3 组蛋白和许多转录因子。不同亚型表达的抑制表明，14-3-3β基因的特异性沉默，而不是γ，显着增加了细胞的成骨潜力。该结果与成骨过程中 14-3-3β Lys 49/51 乙酰化的增加有关。讨论了这种 PTM 在成骨中的可能作用。其中它们的活性状态已被描述为结合 H3 组蛋白和许多转录因子。不同亚型表达的抑制表明，14-3-3β基因的特异性沉默，而不是γ，显着增加了细胞的成骨潜力。该结果与成骨过程中 14-3-3β Lys 49/51 乙酰化的增加有关。讨论了这种 PTM 在成骨中的可能作用。其中它们的活性状态已被描述为结合 H3 组蛋白和许多转录因子。不同亚型表达的抑制表明，14-3-3β基因的特异性沉默，而不是γ，显着增加了细胞的成骨潜力。该结果与成骨过程中 14-3-3β Lys 49/51 乙酰化的增加有关。讨论了这种 PTM 在成骨中的可能作用。

更新日期：2021-08-11

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