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© The Rockefeller University Press, 0021-9525/1998//1349 $5.00
The Journal of Cell Biology, Volume 141, Number 6, , 1998 1349-1356

A Calcium Signaling Cascade Essential for Myosin Thick Filament Assembly in Xenopus Myocytes

Department of Biology and Center for Molecular Genetics, University of California San Diego, La Jolla, California 92093-0357

Spontaneous calcium release from intracellular stores occurs during myofibrillogenesis, the process of sarcomeric protein assembly in striated muscle. Preventing these Ca²⁺ transients disrupts sarcomere formation, but the signal transduction cascade has not been identified. Here we report that specific blockade of Ca²⁺ release from the ryanodine receptor (RyR) activated Ca²⁺ store blocks transients and disrupts myosin thick filament (A band) assembly. Inhibition of an embryonic Ca²⁺/calmodulin-dependent myosin light chain kinase (MLCK) by blocking the ATP-binding site, by allosteric phosphorylation, or by intracellular delivery of a pseudosubstrate peptide, also disrupts sarcomeric organization. The results indicate that both RyRs and MLCK, which have well-described calcium signaling roles in mature muscle contraction, have essential developmental roles during construction of the contractile apparatus.

Abbreviations used in this paper: Bis I, bisindolylmaleimide I; MLCK, myosin light chain kinase; MLCKi, myosin light chain kinase inhibitory peptide; pANT, antennapedia peptide; PKC, protein kinase C; PMA, phorbol 12-myristate, 13-acetate; RLC, regulatory light chain; RyR, ryanodine receptor Ca²⁺ release channel.

K. Ribbeck's present address is Institut fuer Neurobiologie, Universitaet Heidelberg, Im Neuenheimer Feld 345, 69120, Heidelberg, Germany.

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