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首页> 外文期刊>Journal of cell biology >Oxidative stress–induced assembly of PML nuclear bodies controls sumoylation of partner proteins
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Oxidative stress–induced assembly of PML nuclear bodies controls sumoylation of partner proteins

机译：氧化应激诱导的PML核体组装控制伴侣蛋白的磺酰化

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The promyelocytic leukemia (PML) protein organizes PML nuclear bodies (NBs), which are stress-responsive domains where many partner proteins accumulate. Here, we clarify the basis for NB formation and identify stress-induced partner sumoylation as the primary NB function. NB nucleation does not rely primarily on intermolecular interactions between the PML SUMO-interacting motif (SIM) and SUMO, but instead results from oxidation-mediated PML multimerization. Oxidized PML spherical meshes recruit UBC9, which enhances PML sumoylation, allow partner recruitment through SIM interactions, and ultimately enhance partner sumoylation. Intermolecular SUMO–SIM interactions then enforce partner sequestration within the NB inner core. Accordingly, oxidative stress enhances NB formation and global sumoylation in vivo. Some NB-associated sumoylated partners also become polyubiquitinated by RNF4, precipitating their proteasomal degradation. As several partners are protein-modifying enzymes, NBs could act as sensors that facilitate and confer oxidative stress sensitivity not only to sumoylation but also to other post-translational modifications, thereby explaining alterations of stress response upon PML or NB loss.
机译：早幼粒细胞白血病（PML）蛋白组织PML核小体（NBs），这是应激反应域，许多伙伴蛋白在此积聚。在这里，我们澄清了NB形成的基础，并将应力诱导的伴侣sumoylation确定为主要的NB功能。 NB成核作用主要不依赖于PML SUMO相互作用基序（SIM）和SUMO之间的分子间相互作用，而是氧化介导的PML多聚作用导致的。氧化的PML球形网格募集了UBC9，它增强了PML的磺酰化作用，允许通过SIM相互作用募集伴侣，并最终增强了伴侣的磺酰化作用。然后，分子间SUMO-SIM交互作用将强制伙伴隔离在NB内核内。因此，氧化应激增强了体内NB的形成和整体的磺酰化。一些与NB相关的磺酰化伴侣也被RNF4聚泛素化，从而促使其蛋白酶体降解。由于几个伴侣是蛋白质修饰酶，因此，NBs可以充当传感器，不仅促进和赋予氧化应激敏感性，以致磺酰化而且还促进其他翻译后修饰，从而解释了PML或NB丢失后应激反应的改变。

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