Extracellular HSP90 warms up integrins for an irisin workout.
| Autor: | Bourboulia D; 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., Woodford MR; 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., Mollapour M; 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. |
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| Jazyk: | angličtina |
| Zdroj: | Cell metabolism [Cell Metab] 2023 Jul 11; Vol. 35 (7), pp. 1099-1100. Date of Electronic Publication: 2023 Jun 15. |
| DOI: | 10.1016/j.cmet.2023.06.002 |
| Abstrakt: | 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. Competing Interests: Declaration of interests The authors declare no competing financial interests. (Copyright © 2023 Elsevier Inc. All rights reserved.) |
| Databáze: | MEDLINE |
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