Kinetics and mapping of Ca-driven calmodulin conformations on skeletal and cardiac muscle ryanodine receptors

Robyn T. Rebbeck (), Bengt Svensson, Jingyan Zhang, Montserrat Samsó, David D. Thomas, Donald M. Bers and Razvan L. Cornea ()
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Robyn T. Rebbeck: University of Minnesota
Bengt Svensson: University of Minnesota
Jingyan Zhang: University of Minnesota
Montserrat Samsó: Virginia Commonwealth University
David D. Thomas: University of Minnesota
Donald M. Bers: University of California at Davis
Razvan L. Cornea: University of Minnesota

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: Abstract Calmodulin transduces [Ca2+] information regulating the rhythmic Ca2+ cycling between the sarcoplasmic reticulum and cytoplasm during contraction and relaxation in cardiac and skeletal muscle. However, the structural dynamics by which calmodulin modulates the sarcoplasmic reticulum Ca2+ release channel, the ryanodine receptor, at physiologically relevant [Ca2+] is unknown. Using fluorescence lifetime FRET, we resolve different structural states of calmodulin and Ca2+-driven shifts in the conformation of calmodulin bound to ryanodine receptor. Skeletal and cardiac ryanodine receptor isoforms show different calmodulin-ryanodine receptor conformations, as well as binding and structural kinetics with 0.2-ms resolution, which reflect different functional roles of calmodulin. These FRET methods provide insight into the physiological calmodulin-ryanodine receptor structural states, revealing additional distinct structural states that complement cryo-EM models that are based on less physiological conditions. This technology will drive future studies on pathological calmodulin-ryanodine receptor interactions and dynamics with other important ryanodine receptor bound modulators.

Date: 2024
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DOI: 10.1038/s41467-024-48951-5

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