Loss of S100A1 expression leads to Ca2+ release potentiation in mutant mice with disrupted CaM and S100A1 binding to CaMBD2 of RyR1

Loss of S100A1 expression leads to Ca2+ release potentiation in mutant mice with disrupted CaM and S100A1 binding to CaMBD2 of RyR1

Abstract Calmodulin (CaM) and S100A1 fine‐tune skeletal muscle Ca2+ release via opposite modulation of the ryanodine receptor type 1 (RyR1). Binding to and modulation of RyR1 by CaM and S100A1 occurs predominantly at the region ranging from amino acid residue 3614‐3640 of RyR1 (here referred to as C...

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Bibliographic Details
Main Authors: Erick O. Hernández‐Ochoa, Zephan Melville, Camilo Vanegas, Kristen M. Varney, Paul T. Wilder, Werner Melzer, David J. Weber, Martin F. Schneider
Format: Article
Language:English
Published: Wiley 2018-08-01
Series:Physiological Reports
Subjects:
Ca2+ release
calmodulin
excitation‐contraction coupling
isothermal calorimetry
RyR1
S100A1
Online Access:https://doi.org/10.14814/phy2.13822

Internet

https://doi.org/10.14814/phy2.13822

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