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Structure and function of the AAA + ATPase p97/Cdc48p

机译:AAA + ATPase p97 / Cdc48p的结构和功能

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p97 (also known as valosin-containing protein (VCP) in mammals or Cdc48p in Saccharomyces cerevisiae) is an evolutionarily conserved ATPase present in all eukaryotes and archaebacteria. In conjunction with a collection of cofactors and adaptors, p97/Cdc48p performs an array of biological functions mostly through modulating the stability of 'client' proteins. Using energy from ATP hydrolysis, p97/Cdc48p segregates these molecules from immobile cellular structures such as protein assemblies, membrane organelles, and chromatin. Consequently, the released polypeptides can be efficiently degraded by the ubiquitin proteasome system or recycled. This review summarizes our current understanding of the structure and function of this essential cellular chaperoning system. Published by Elsevier B.V.
机译:p97(在哺乳动物中也称为含缬氨酸的蛋白质(VCP),在酿酒酵母中也称为Cdc48p)是存在于所有真核生物和古细菌中的一种进化保守的ATPase。与辅因子和衔接子的集合一起,p97 / Cdc48p主要通过调节“客户”蛋白的稳定性来执行一系列生物学功能。利用来自ATP水解的能量,p97 / Cdc48p将这些分子与固定的细胞结构(例如蛋白质装配体,膜细胞器和染色质)分离。因此,释放的多肽可被泛素蛋白酶体系统有效降解或再循环。这篇综述总结了我们目前对该基本细胞伴侣系统的结构和功能的理解。由Elsevier B.V.发布

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