Cargando…
Calmodulin Binding to the 3614–3643 Region of RyR1 Is Not Essential for Excitation–Contraction Coupling in Skeletal Myotubes
Calmodulin is a ubiquitous Ca(2+) binding protein that modulates the in vitro activity of the skeletal muscle ryanodine receptor (RyR1). Residues 3614–3643 of RyR1 comprise the CaM binding domain and mutations within this region result in a loss of both high-affinity Ca(2+)-bound calmodulin (CaCaM)...
Autores principales: | O'Connell, Kristen M.S., Yamaguchi, Naohiro, Meissner, Gerhard, Dirksen, Robert T. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2002
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2229515/ https://www.ncbi.nlm.nih.gov/pubmed/12198090 http://dx.doi.org/10.1085/jgp.20028617 |
Ejemplares similares
-
Zinc controls RyR2 activity during excitation-contraction coupling
por: Stewart, Alan J, et al.
Publicado: (2015) -
Ca(2+)-dependent calmodulin binding to cardiac ryanodine receptor (RyR2) calmodulin-binding domains
por: Brohus, Malene, et al.
Publicado: (2019) -
Structure of RyR1 in native membranes
por: Chen, Wenbo, et al.
Publicado: (2020) -
Identification of RyR2-PBmice and the effects of transposon insertional mutagenesis of the RyR2 gene on cardiac function in mice
por: Wang, Qianqian, et al.
Publicado: (2019) -
A Structural Model of the Pore-Forming Region of the Skeletal Muscle Ryanodine Receptor (RyR1)
por: Ramachandran, Srinivas, et al.
Publicado: (2009)