p97：细胞的分子炼狱？

p97: The cell's molecular purgatory?

作者信息

Halawani Dalia, Latterich Martin

机构信息

Department of Anatomy and Cell Biology, McGill University, 3640 University Street, Montreal, QC H3A 2B2, Canada.

出版信息

Mol Cell. 2006 Jun 23;22(6):713-717. doi: 10.1016/j.molcel.2006.06.003.

DOI:10.1016/j.molcel.2006.06.003

PMID:16793541

Abstract

The multifunctional AAA-ATPase p97/VCP is one of the most extensively studied members of this protein family, yet it presents the field with many perplexing questions surrounding its mechanism of substrate engagement and processing. Recent discoveries have unmasked a new purgatorial identity for this molecule in the ubiquitin-proteasome pathway, specifically its role in linking ubiquitylated substrates with competing ubiquitin conjugation and deconjugation machineries. Furthermore, biochemical studies surprisingly identify the C-terminal D2 ring as essential for substrate interaction, thus bringing p97 one step closer to its prokaryotic AAA protease relatives.

摘要

多功能AAA-ATP酶p97/VCP是该蛋白家族中研究最为广泛的成员之一，但它在底物结合和加工机制方面给该领域带来了许多令人困惑的问题。最近的发现揭示了该分子在泛素-蛋白酶体途径中的一种新的中间作用，特别是其在将泛素化底物与竞争性泛素结合和去结合机制联系起来方面的作用。此外，生化研究令人惊讶地发现C末端D2环对于底物相互作用至关重要，从而使p97与其原核AAA蛋白酶亲属的关系更近了一步。