Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions
Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions
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DOI：
10.1016/j.jsb.2003.11.014
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发表时间：
2004-04-01
影响因子：
3
通讯作者：
Li, CCH
中科院分区：
文献类型：
--
作者：
Wang, Q;Song, CC;Li, CCH
含有 97-kDa valosin 的蛋白（p97 或 VCP）是 II 型 AAA（(A) over bar TPases (a) over bar 与多种 (a) over bar 活性相关) ATPase，其特征在于拥有两个保守的 ATPase 结构域。 VCP形成稳定的同源六聚体结构，这种两层环形复合物充当分子伴侣，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辅因子的鉴定为我们了解这种分子伴侣的工作原理提供了重要线索。在这篇综述中，我们总结了已报道的 VCP 生物学功能，并探讨了不同细胞功能背后的分子机制。我们讨论了结构和生化研究，并阐明了这种复杂的酶机器如何将化学能转化为伴侣活动所需的机械力。由爱思唯尔公司出版
The 97-kDa valosin-containing protein (p97 or VCP) is a type-II AAA ((A) over bar TPases (a) over bar ssociated with a variety of (a) over bar ctivities) 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. Published by Elsevier Inc.