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The proteasome maturation protein POMP facilitates major steps of 20S proteasome formation at the endoplasmic reticulum

机译:蛋白酶体成熟蛋白POMP促进内质网20S蛋白酶体形成的主要步骤

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摘要

The quality control of proteins mediated by the plasticity of the proteasome system is regulated by the timely and flexible formation of this multisubunit proteolytic enzyme complex. Adaptable biogenesis of the 20S proteasome core complex is therefore of vital importance for adjusting to changing proteolytic requirements. However, the molecular mechanism and the cellular sites of mammalian proteasome formation are still unresolved. By using precursor complex-specific antibodies, we now show that the main steps in 20S core complex formation take place at the endoplasmic reticulum (ER). Thereby, the proteasome maturation protein (POMP)—an essential factor of mammalian proteasome biogenesis—interacts with ER membranes, binds to α1–7 rings, recruits β-subunits stepwise and mediates the association of mammalian precursor complexes with the ER. Thus, POMP facilitates the main steps in 20S core complex formation at the ER to coordinate the assembly process and to provide cells with freshly formed proteasomes at their site of function.
机译:由蛋白酶体系统的可塑性介导的蛋白质的质量控制由该多亚基蛋白水解酶复合物的及时而灵活的形成来调节。因此,20S蛋白酶体核心复合物的适应性生物发生对于适应不断变化的蛋白水解需求至关重要。但是,哺乳动物蛋白酶体形成的分子机制和细胞位置仍未解决。通过使用前体复合物特异性抗体,我们现在显示20S核心复合物形成的主要步骤发生在内质网(ER)。因此,蛋白酶体成熟蛋白(POMP)-哺乳动物蛋白酶体生物发生的重要因素-与ER膜相互作用,与α1–7环结合,逐步募集β亚基,并介导了哺乳动物前体复合物与ER的缔合。因此,POMP促进了ER处20S核心复合物形成的主要步骤,以协调组装过程并在其功能部位为细胞提供新鲜形成的蛋白酶体。

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