Tudor-dimethylarginine interactions: the condensed version.
Tudor-dimethylarginine interactions: the condensed version.
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DOI：
10.1016/j.tibs.2023.04.003
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发表时间：
2023-05
影响因子：
13.8
通讯作者：
Daniela Šimčíková;Sara Gelles-Watnick;K. Neugebauer
中科院分区：
文献类型：
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作者：
Daniela Šimčíková;Sara Gelles-Watnick;K. Neugebauer
生物分子凝聚物（BMC）可以促进或抑制多种细胞功能。BMC的形成是由非共价蛋白质-蛋白质、蛋白质-RNA和RNA-RNA相互作用驱动的。在这里，我们专注于Tudor结构域的蛋白质-如运动神经元生存蛋白（SMN）-有助于BMC的形成结合二甲基精氨酸（DMA）修饰蛋白质配体。SMN存在于富含RNA的BMC中，其缺失导致脊髓性肌萎缩症（SMA）。SMN的Tudor结构域形成细胞质和细胞核BMC，但其DMA配体在很大程度上是未知的，突出了关于SMN功能的开放性问题。此外，DMA修饰可以改变分子内相互作用并影响蛋白质定位。尽管有这些新兴的功能，但缺乏直接的DMA检测方法仍然是理解细胞中Tudor-DMA相互作用的障碍。
Biomolecular condensates (BMCs) can facilitate or inhibit diverse cellular functions. BMC formation is driven by noncovalent protein–protein, protein–RNA, and RNA–RNA interactions. Here, we focus on Tudor domain-containing proteins – such as survival motor neuron protein (SMN) – that contribute to BMC formation by binding to dimethylarginine (DMA) modifications on protein ligands. SMN is present in RNA-rich BMCs, and its absence causes spinal muscular atrophy (SMA). SMN's Tudor domain forms cytoplasmic and nuclear BMCs, but its DMA ligands are largely unknown, highlighting open questions about the function of SMN. Moreover, DMA modification can alter intramolecular interactions and affect protein localization. Despite these emerging functions, the lack of direct methods of DMA detection remains an obstacle to understanding Tudor–DMA interactions in cells.