Wang Qing, Song Changcheng, Li Chou-Chi H
Basic Research Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702, USA.
J Struct Biol. 2004 Apr-May;146(1-2):44-57. doi: 10.1016/j.jsb.2003.11.014.
The 97-kDa valosin-containing protein (p97 or VCP) is a type-II AAA ( ATPases associated with a variety of activities) ATPases, which are characterized by possessing two conserved ATPase domains. VCP forms a stable homo-hexameric structure, and this two-tier ring-shaped complex acts as a molecular chaperone that mediates many seemingly unrelated cellular activities. The involvement of VCP in the ubiquitin-proteasome degradation pathway and the identification of VCP cofactors provided us important clues to the understanding of how this molecular chaperone works. In this review, we summarize the reported biological functions of VCP and explore the molecular mechanisms underlying the diverse cellular functions. We discuss the structural and biochemical studies, and elucidate how this sophisticated enzymatic machine converts chemical energy into the mechanical forces required for the chaperone activity.
97千道尔顿含缬酪肽蛋白（p97或VCP）是一种II型AAA（与多种活动相关的ATP酶）ATP酶，其特征是拥有两个保守的ATP酶结构域。VCP形成稳定的同型六聚体结构，这种双层环形复合物作为分子伴侣介导许多看似不相关的细胞活动。VCP参与泛素-蛋白酶体降解途径以及VCP辅助因子的鉴定为我们理解这种分子伴侣的工作方式提供了重要线索。在本综述中，我们总结了已报道的VCP的生物学功能，并探讨了其多样细胞功能背后的分子机制。我们讨论了结构和生化研究，并阐明了这种精密的酶机器如何将化学能转化为伴侣活性所需的机械力。
