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Regulation of Protein Transport Pathways by the Cytosolic Hsp90s
Anna G Mankovich1, Brian C Freeman1
1School of Molecular and Cellular Biology, University of Illinois, Urbana-Champaign, Urbana, IL 61801, USA.
Biomolecules
|August 26, 2022
Summary
Heat shock protein 90 (Hsp90) plays a key role in protein transport, influencing pathways like vesicular transport and protein secretion. Understanding Hsp90
Area of Science:
- Molecular biology
- Cellular dynamics
- Protein trafficking
Background:
- Heat shock protein 90 (Hsp90) is a crucial molecular chaperone involved in protein homeostasis and intracellular dynamics.
- High-throughput interactome studies reveal Hsp90's association with diverse cellular pathways beyond its known chaperone functions.
Purpose of the Study:
- To investigate the potential role and impact of Hsp90 in various protein transport mechanisms.
- To explore the unresolved connections between Hsp90 and factors involved in protein transport pathways.
Main Methods:
- Review and analysis of existing literature and high-throughput interactome data.
- Identification of Hsp90 interactors relevant to protein transport processes.
Main Results:
- Hsp90 interacts with numerous factors implicated in endocytic/exocytic vesicular transport, transmembrane polypeptide transfer, and unconventional protein secretion.
- A limited number of mechanistic contributions of Hsp90 to protein transport have been defined, leaving many connections unresolved.
Conclusions:
- Hsp90 likely plays a significant, yet underappreciated, role in diverse protein transport pathways.
- Elucidating Hsp90's function in protein transport could yield novel therapeutic targets for diseases such as cancer, infections, and neurodegeneration.
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