ArticleBiophysical journal2006
Role of the Met3534-Ala4271 region of the ryanodine receptor in the regulation of Ca2+ release induced by calmodulin binding domain peptide.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 17 citations in OpenAlex.
- Structural Insight Into Ryanodine Receptor Channelopathies.Frontiers in pharmacology · 2022Review
- Activation of IP3 receptors requires an endogenous 1-8-14 calmodulin-binding motif.The Biochemical journal · 2013Article
- Aberrant interaction of calmodulin with the ryanodine receptor develops hypertrophy in the neonatal cardiomyocyte.The Biochemical journal · 2011Article
- Dissociation of calmodulin from cardiac ryanodine receptor causes aberrant Ca(2+) release in heart failure.Cardiovascular research · 2010Article
- Calmodulin in adult mammalian skeletal muscle: localization and effect on sarcoplasmic reticulum Ca2+ release.American journal of physiology. Cell physiology · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
CaMBP, a peptide corresponding to the 3614-3643 calmodulin (CaM) binding region of the ryanodine receptor (RyR1), is known to activate RyR1 Ca2+ channel. To analyze the mechanism of channel regulation by the CaMBP-RyR1 interaction, we investigated a), CaMBP binding to RyR1, b), induced local conformational changes in the CaMBP binding region of RyR1 using the fluorescent conformational probe badan attached to CaMBP (CaMBP-badan), and c), effects of "a" and "b" on SR Ca2+ release. We also monitored the interaction of CaMBP-badan with CaM and a peptide corresponding to the Met3534-Ala4271 region of RyR1 (R3534-4271) as a control. At lower peptide concentrations (< or =15 microM), CaMBP binding to RyR1 increased the intensity of badan fluorescence emission at a shorter wavelength (the state resembling CaMBP-badan/Ca-CaM) and induced Ca2+ release. Further increase in CaMBP concentration (up to approximately 50 microM) produced more binding of CaMBP accompanied by further increase in the badan fluorescence emission but at a longer wavelength (the state resembling CaMBP-badan/apo-CaM) and inhibited Ca2+ release. Binding of CaMBP-badan to R3534-4271 increased the intensity of badan fluorescence, showing the similar concentration-dependent red-shift of the emission maximum. It is proposed that CaMBP interacts with two classes of binding sites located in the Met3534-Ala4271 region of RyR1, which activate and inhibit the Ca2+ channel, respectively.
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