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Extracellular HSP90 warms up integrins for an irisin workout
Dimitra Bourboulia1, Mark R Woodford1, Mehdi Mollapour1
1Department of Urology, SUNY Upstate Medical University, Syracuse, NY 13210, USA; Upstate Cancer Center, SUNY Upstate Medical University, Syracuse, NY 13210, USA; Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, Syracuse, NY 13210, USA.
Cell Metabolism
|June 16, 2023
Summary
Irisin, a metabolism-regulating protein, requires heat shock protein-90 (Hsp90) to activate the αVβ5 integrin receptor. This activation enables irisin binding and signal transduction for improved metabolic regulation.
Area of Science:
- Metabolic regulation
- Cell signaling
- Protein interactions
Background:
- Irisin is a hormone-like protein crucial for adipose tissue browning and metabolic control.
- Understanding irisin's mechanism of action is key to metabolic research.
Purpose of the Study:
- To identify the factors that regulate irisin's interaction with its receptor.
- To elucidate the mechanism of irisin-mediated signal transduction.
Main Methods:
- Investigated the role of extracellular chaperones in irisin signaling.
- Focused on the interaction between irisin and the αVβ5 integrin receptor.
Main Results:
- Heat shock protein-90 (Hsp90) was identified as the activating factor for the αVβ5 integrin receptor.
- Hsp90 facilitates the "opening" of αVβ5 integrin, enabling high-affinity irisin binding.
- This interaction is essential for effective irisin signal transduction.
Conclusions:
- Hsp90 plays a critical role in mediating irisin's effects on metabolism.
- The Hsp90-αVβ5 integrin interaction is a novel target for modulating irisin activity.
- Findings provide new insights into the molecular mechanisms of metabolic regulation.
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