Extracellular HSP90 warms up integrins for an irisin workout

Dimitra Bourboulia; Mark R Woodford; Mehdi Mollapour

doi:10.1016/j.cmet.2023.06.002

Extracellular HSP90 warms up integrins for an irisin workout

Cell Metab. 2023 Jul 11;35(7):1099-1100. doi: 10.1016/j.cmet.2023.06.002. Epub 2023 Jun 15.

Authors

Dimitra Bourboulia¹, Mark R Woodford², Mehdi Mollapour³

Affiliations

¹ Department 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. Electronic address: bourmpod@upstate.edu.
² Department 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. Electronic address: woodform@upstate.edu.
³ Department 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. Electronic address: mollapom@upstate.edu.

Abstract

The hormone-like protein irisin is involved in browning of adipose tissue and regulation of metabolism. Recently, Mu et al. identified the extracellular chaperone heat shock protein-90 (Hsp90) as the activating factor for "opening" αVβ5 integrin receptor, allowing for high-affinity irisin binding and effective signal transduction.

Publication types

Research Support, N.I.H., Extramural
Comment

MeSH terms

Adipose Tissue / metabolism
Fibronectins* / metabolism
HSP90 Heat-Shock Proteins / metabolism
Integrins*
Signal Transduction

Substances

Fibronectins
Integrins
HSP90 Heat-Shock Proteins

Abstract

Publication types

MeSH terms

Substances

Grants and funding