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The Journal of Experimental Biology 206, 1899-1906 (2003)
doi: 10.1242/jeb.00377

The pathway of myofibrillogenesis determines the interrelationship between myosin and paramyosin synthesis in Caenorhabditis elegans

Glenn E. White^*, Christine M. Petry and Fred Schachat

Department of Cell Biology – Box 3011, Duke University Medical School, Durham, NC 27710, USA
^* Present address: Department of Biology, University of North Carolina – Asheville, Asheville, NC 28804, USA

Author for correspondence (e-mail: f.schachat{at}cellbio.duke.edu)

Accepted 17 March 2003

Examination of null mutants in myosin B and paramyosin yields insights into the complex mechanisms that regulate expression of the three major components of Caenorhabditis elegans body-wall muscle thick filaments myosin A, myosin B and paramyosin. In the absence of myosin B, paramyosin accumulation is reduced, although neither its synthesis nor that of myosin A is affected. This implies that the interaction of myosin B with paramyosin inhibits paramyosin degradation. By contrast, the absence of paramyosin results in reduced synthesis and accumulation of myosin B but has no effect on myosin A synthesis. The non-reciprocal effects of the null mutants on turnover and synthesis are best understood as an epigenetic phenomenon that reflects the pathway of thick filament assembly. The synthesis of myosin A and paramyosin, which are involved in the initial steps of thick filament formation, is independent of myosin B; however, a properly assembled paramyosin-containing thick filament core is essential for efficient synthesis of myosin B.

Key words: myosin B, myosin A, paramyosin, Caenorhabditis elegans, mutant, thick filament, myofibrillogenesis

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