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Impairment of muscle function caused by mutations of phosphorylation sites in myosin regulatory light chain

Nature volume 374, pages 650–653 (1995)Cite this article

Abstract

MYOSIN regulatory light chain is phosphorylated by myosin light chain kinase at conserved serine and threonine residues in a number of species1. Phosphorylation of myosin regulatory light chain regulates smooth muscle contraction, but appears to have a modulatory role in striated muscle contraction2. We assessed the in vivo role of myosin regulatory light chain phosphorylation in the striated muscles of Drosophila melanogaster by substituting alanine at each or both conserved myosin light chain kinase-dependent phosphorylation sites, serine 66 and serine 67. We report here that myosin light chain kinase-dependent phosphorylation is not required for myofibrillogenesis or for the development of maximal isometric force in indirect flight muscles. However, mutants with substitutions at the major phosphorylation site (serine 66) or with the double substitutions had reduced power output in isolated flight muscle fibres and reduced flight ability, showing that myosin regulatory light chain phosphorylation is a key determinant of the stretch activation response in Drosophila.

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Authors and Affiliations

  1. Department of Molecular Genetics, The Ohio State University, Columbus, Ohio, 43210, USA

    Rutaiwan Tohtong, Melissa Graham & Amanda Simcox

  2. Department of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont, 05405, USA

    Hiroshi Yamashita, Joe Haeberle & David Maughan

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  1. Rutaiwan Tohtong
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  2. Hiroshi Yamashita
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  3. Melissa Graham
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  4. Joe Haeberle
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Tohtong, R., Yamashita, H., Graham, M. et al. Impairment of muscle function caused by mutations of phosphorylation sites in myosin regulatory light chain. Nature 374, 650–653 (1995). https://doi.org/10.1038/374650a0

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