Description
Title: Cytosolic Hsp90s regulate protein transport pathways
Abstract: Heat shock protein 90 (Hsp90), a highly conserved molecular chaperone, is well known for preserving metastable proteins and mediating a variety of intracellular protein dynamics. It’s interesting to note that high-throughput interactome studies indicate that Hsp90 is connected to numerous other pathways. Here, we’ll focus on Hsp90’s potential role in protein transport. The relevance of hundreds of additional connections between Hsp90 and factors known to facilitate this process remains unresolved, despite the fact that a relatively small number of studies have identified a few of the mechanistic contributions of Hsp90 to protein transport. These interactors support a variety of transport mechanisms, such as the translocation of polypeptides across membranes, endocytic and exocytic vesicular transport, and unusual protein secretion. New therapeutic targets will likely be found for the treatment of many human health problems, such as bacterial infection, cancer metastasis, and neurodegeneration, as a result of determining how Hsp90 participates in the protein transport process.
Keywords: Hsp90; molecular chaperone; protein transport
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Biomolecules
Writer Experience: 20+ Years
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