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首页> 外文期刊>Cell cycle >HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor of the Cul4-DDB1 ubiquitin ligase.
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HIV1 Vpr arrests the cell cycle by recruiting DCAF1/VprBP, a receptor of the Cul4-DDB1 ubiquitin ligase.

机译：HIV1 Vpr通过募集Cul4-DDB1泛素连接酶的受体DCAF1 / VprBP来阻止细胞周期。

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摘要

How the HIV1 Vpr protein initiates the host cell response leading to cell cycle arrest in G(2) has remained unknown. Here, we show that recruitment of DCAF1/VprBP by Vpr is essential for its cytostatic activity, which can be abolished either by single mutations of Vpr that impair DCAF1 binding, or by siRNA-mediated silencing of DCAF1. Furthermore, DCAF1 bridges Vpr to DDB1, a core subunit of Cul4 ubiquitin ligases. Altogether these results point to a mechanism where Vpr triggers G(2) arrest by hijacking the Cul4/DDB1(DCAF1) ubiquitin ligase. We further show that, Vpx, a non-cytostatic Vpr-related protein acquired by HIV2 and SIV, also binds DCAF1 through a conserved motif. Thus, Vpr from HIV1 and Vpx from SIV recruit DCAF1 with different physiological outcomes for the host cell. This in turn suggests that both proteins have evolved to preserve interaction with the same Cul4 ubiquitin ligase while diverging in the recognition of host substrates targeted for proteasomal degradation.
机译：HIV1 Vpr蛋白如何引发宿主细胞反应导致细胞周期停滞在G（2）仍然未知。在这里，我们显示Vpr募集DCAF1 / VprBP对于其细胞抑制活性至关重要，这可以通过破坏DCAF1结合的Vpr单个突变或通过siRNA介导的DCAF1沉默来消除。此外，DCAF1将Vpr桥接到DDB1，DDB1是Cul4泛素连接酶的核心亚基。总而言之，这些结果表明Vpr通过劫持Cul4 / DDB1（DCAF1）泛素连接酶来触发G（2）逮捕。我们进一步表明，Vpx，由HIV2和SIV获得的非细胞抑制性Vpr相关蛋白，也通过保守的基序结合DCAF1。因此，来自HIV1的Vpr和来自SIV的Vpx募集了对宿主细胞具有不同生理结果的DCAF1。这又表明这两种蛋白质已经进化为保留与相同的Cul4泛素连接酶的相互作用，同时在针对蛋白酶体降解的宿主底物的识别上有所差异。

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