ArticleBiophysical chemistry
Calcium-dependent energetics of calmodulin domain interactions with regulatory regions of the Ryanodine Receptor Type 1 (RyR1).
Article in Biophysical chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Remodeling of the ryanodine receptor isoform 1 channel regulates the sweet and umami taste perception ofFundamental research · 2023Article
- NaStructure (London, England : 1993) · 2021Article
- Deletion of Fibroblast growth factor 9 globally and in skeletal muscle results in enlarged tuberosities at sites of deltoid tendon attachments.Developmental dynamics : an official publication of the American Association of Anatomists · 2021Article
- Resolved Structural States of Calmodulin in Regulation of Skeletal Muscle Calcium Release.Biophysical journal · 2020Article
- Structural dynamics of calmodulin-ryanodine receptor interactions: electron paramagnetic resonance using stereospecific spin labels.Scientific reports · 2018Article
- Calcium-Dependent Structural Dynamics of a Spin-Labeled RyR Peptide Bound to Calmodulin.Biophysical journal · 2016Article
- Multifaceted Roles of ALG-2 in Ca(2+)-Regulated Membrane Trafficking.International journal of molecular sciences · 2016Review
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4 authors.
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Abstract
Calmodulin (CaM) allosterically regulates the homo-tetrameric human Ryanodine Receptor Type 1 (hRyR1): apo CaM activates the channel, while (Ca(2+))4-CaM inhibits it. CaM-binding RyR1 residues 1975-1999 and 3614-3643 were proposed to allow CaM to bridge adjacent RyR1 subunits. Fluorescence anisotropy titrations monitored the binding of CaM and its domains to peptides encompassing hRyR(11975-1999) or hRyR1(3614-3643). Both CaM and its C-domain associated in a calcium-independent manner with hRyR1(3614-3643) while N-domain required calcium and bound ~250-fold more weakly. Association with hRyR1(11975-1999) was weak. Both hRyR1 peptides increased the calcium-binding affinity of both CaM domains, while maintaining differences between them. These energetics support the CaM C-domain association with hRyR1(3614-3643) at low calcium, positioning CaM to respond to calcium efflux. However, the CaM N-domain affinity for hRyR(11975-1999) alone was insufficient to support CaM bridging adjacent RyR1 subunits. Other proteins or elements of the hRyR1 structure must contribute to the energetics of CaM-mediated regulation.
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