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Ronjat et al. (1) report that a phosphorylated form of the scorpion venom toxin maurocalcin (MCa) loses its ability to activate its preferred target, the type 1 ryanodine receptor (RYR1). RYR1 is the sarcoplasmic reticulum (SR) Ca2+ release channel responsible for the rise in cytosolic Ca2+, which activates contraction during excitation–contraction coupling of skeletal muscle. Ronjat et al. report that phosphorylation of MCa threonine 26 (MCaThr26) completely reprograms the toxin, converting it into a RYR1 blocker. To assess the function of MCa and of MCaThr26-Phospho, the authors relied on several in vitro assays, including measurements of current through RYR1 channels reconstituted into lipid bilayer and [3H]-ryanodine binding and Ca2+ release from SR vesicles. However, Ronjat et al. did not obtain data from intact muscle fibers where RYR1 functions in its native physiological environment, being activated by its molecular partner, the voltage-sensing protein CAV1.1 in the plasma membrane. This is unfortunate because MCa … [↵][1]1To whom correspondence should be addressed. Email: vincent.jacquemond{at}univ-lyon1.fr. [1]: #xref-corresp-1-1

Maurocalcin phosphorylated at threonin 26 maintains its activity on ryanodine receptor-mediated Ca 2+ release in intact muscle fibers

Maurocalcin phosphorylated at threonin 26 maintains its activity on ryanodine receptor-mediated Ca ²⁺ release in intact muscle fibers