Unveiling the intricate role of S100A1 in regulating RyR1 activity: A commentary on "Structural insights into the regulation of RyR1 by S100A1".

Autor: Perry ML; Department of Biochemistry & Molecular Biology School of Medicine University of Maryland, Baltimore, MD, USA., Varney KM; Department of Biochemistry & Molecular Biology School of Medicine University of Maryland, Baltimore, MD, USA; Center for Biomolecular Therapeutics (CBT), Baltimore, MD, USA; Institute of Bioscience and Biotechnology Research (IBBR), Rockville, MD, USA., Tiwary P; Department of Biochemistry & Molecular Biology School of Medicine University of Maryland, Baltimore, MD, USA; Department of Chemistry & Biochemistry and Institute for Physical Science & Technology, University of Maryland, College Park, MD, USA; University of Maryland Institute for Health Computing, Bethesda, MD 20852, USA., Weber DJ; Department of Biochemistry & Molecular Biology School of Medicine University of Maryland, Baltimore, MD, USA; Center for Biomolecular Therapeutics (CBT), Baltimore, MD, USA; Institute of Bioscience and Biotechnology Research (IBBR), Rockville, MD, USA; Department of Chemistry & Biochemistry and Institute for Physical Science & Technology, University of Maryland, College Park, MD, USA., Hernández-Ochoa EO; Department of Biochemistry & Molecular Biology School of Medicine University of Maryland, Baltimore, MD, USA. Electronic address: ehernandez-ochoa@som.umaryland.edu.
Jazyk: angličtina
Zdroj: Cell calcium [Cell Calcium] 2024 Nov; Vol. 123, pp. 102947. Date of Electronic Publication: 2024 Aug 23.
DOI: 10.1016/j.ceca.2024.102947
Abstrakt: S100A1, a calcium-binding protein, plays a crucial role in regulating Ca 2+ signaling pathways in skeletal and cardiac myocytes via interactions with the ryanodine receptor (RyR) to affect Ca 2+ release and contractile performance. Biophysical studies strongly suggest that S100A1 interacts with RyRs but have been inconclusive about both the nature of this interaction and its competition with another important calcium-binding protein, calmodulin (CaM). Thus, high-resolution cryo-EM studies of RyRs in the presence of S100A1, with or without additional CaM, were needed. The elegant work by Weninger et al. demonstrates the interaction between S100A1 and RyR1 through various experiments and confirms that S100A1 activates RyR1 at sub-micromolar Ca 2+ concentrations, increasing the open probability of RyR1 channels.
Competing Interests: Declaration of competing interest The authors declare no conflict of interest.
(Copyright © 2024. Published by Elsevier Ltd.)
Databáze: MEDLINE
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