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首页> 外文期刊>Nature >The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase
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The BTB protein MEL-26 is a substrate-specific adaptor of the CUL-3 ubiquitin-ligase

机译：BTB蛋白MEL-26是CUL-3泛素连接酶的底物特异性衔接子

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摘要

Many biological processes, such as development and cell cycle progression are tightly controlled by selective ubiquitin-depen-dent degradation of key substrates. In this pathway, the E3-ligase recognizes the substrate and targets it for degradation by the 26S proteasome. The SCF (Skp1―Cul1―F-box) and ECS (Elongin C―Cul2―SOCS box) complexes are two well-defined cullin-based E3-ligases. The cullin subunits serve a scaffolding function and interact through their C terminus with the RING-finger-contain-ing protein Hrt1/Roc1/Rbx1, and through their N terminus with Skp1 or Elongin C, respectively. In Caenorhabditis elegans, the ubiquitin-ligase activity of the CUL-3 complex is required for degradation of the microtubule-severing protein MEI-1/katanin at the meiosis-to-mitosis transition. However, the molecular composition of this cullin-based E3-ligase is not known. Here we identified the BTB-containing protein MEL-26 as a component required for degradation of MEI-1 in vivo. Importantly, MEL-26 specifically interacts with CUL-3 and MEI-1 in vivo and in vitro, and displays properties of a substrate-specific adaptor. Our results suggest that BTB-containing proteins may generally function as substrate-specific adaptors in Cul3-based E3-ubiqui-tin ligases.
机译：许多生物学过程，例如发育和细胞周期进程，都受到关键底物选择性泛素依赖性降解的严格控制。在该途径中，E3-连接酶识别底物，并将其靶向26S蛋白酶体降解。 SCF（Skp1–Cul1–F-box）和ECS（Elongin C–Cul2–SOCS box）复合物是两种基于cullin的E3连接酶。 cullin亚基具有脚手架功能，并通过其C末端与RING手指蛋白Hrt1 / Roc1 / Rbx1相互作用，并通过其N末端与Skp1或Elongin C相互作用。在秀丽隐杆线虫中，CUL-3复合体的泛素-连接酶活性是在减数分裂向有丝分裂过渡时降解微管切割蛋白MEI-1 / katanin所必需的。然而，这种基于cullin的E3-连接酶的分子组成是未知的。在这里，我们确定了含有BTB的蛋白质MEL-26是在体内降解MEI-1所需的组分。重要的是，MEL-26在体内和体外与CUL-3和MEI-1特异性相互作用，并显示底物特异性衔接子的特性。我们的结果表明，含BTB的蛋白质通常可以在基于Cul3的E3泛素连接酶中充当底物特异性衔接子。

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