School of Molecular and Cellular Biology, University of Illinois, Urbana-Champaign, Urbana, IL 61801, USA.
Biomolecules. 2022 Aug 5;12(8):1077. doi: 10.3390/biom12081077.
The highly conserved molecular chaperone heat shock protein 90 (Hsp90) is well-known for maintaining metastable proteins and mediating various aspects of intracellular protein dynamics. Intriguingly, high-throughput interactome studies suggest that Hsp90 is associated with a variety of other pathways. Here, we will highlight the potential impact of Hsp90 in protein transport. Currently, a limited number of studies have defined a few mechanistic contributions of Hsp90 to protein transport, yet the relevance of hundreds of additional connections between Hsp90 and factors known to aide this process remains unresolved. These interactors broadly support transport pathways including endocytic and exocytic vesicular transport, the transfer of polypeptides across membranes, or unconventional protein secretion. In resolving how Hsp90 contributes to the protein transport process, new therapeutic targets will likely be obtained for the treatment of numerous human health issues, including bacterial infection, cancer metastasis, and neurodegeneration.
高度保守的分子伴侣热休克蛋白 90（Hsp90）是众所周知的维持亚稳态蛋白，并介导细胞内蛋白质动力学的各个方面。有趣的是，高通量互作组学研究表明，Hsp90与多种其他途径有关。在这里，我们将重点介绍 Hsp90 在蛋白质运输中的潜在作用。目前，只有少数研究定义了 Hsp90 在蛋白质运输中的几种机制贡献，然而，Hsp90 与已知有助于这一过程的数百种其他因子之间的相关性仍未得到解决。这些相互作用体广泛支持包括内吞和外排小泡运输、跨膜多肽转移或非传统蛋白质分泌在内的运输途径。在确定 Hsp90 如何促进蛋白质运输过程中，可能会获得新的治疗靶点，以治疗许多人类健康问题，包括细菌感染、癌症转移和神经退行性变。
