Xia Di, Tang Wai Kwan, Ye Yihong
Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, United States.
Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, United States.
Gene. 2016 May 25;583(1):64-77. doi: 10.1016/j.gene.2016.02.042. Epub 2016 Mar 3.
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.
p97（在哺乳动物中也称为含缬酪肽蛋白（VCP），在酿酒酵母中称为Cdc48p）是一种在所有真核生物和古细菌中都存在的进化保守的ATP酶。与一系列辅助因子和衔接蛋白协同作用，p97/Cdc48p主要通过调节“底物”蛋白的稳定性来执行一系列生物学功能。利用ATP水解产生的能量，p97/Cdc48p将这些分子与固定的细胞结构（如蛋白质聚集体、膜细胞器和染色质）分离。因此，释放的多肽可以被泛素蛋白酶体系统有效降解或再循环利用。本综述总结了我们目前对这个重要细胞伴侣系统的结构和功能的理解。
