4.5 Article

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

Journal

JOURNAL OF EXPERIMENTAL BIOLOGY
Volume 206, Issue 11, Pages 1899-1906

Publisher

COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jeb.00377

Keywords

myosin B; myosin A; paramyosin; Caenorhabditis elegans; mutant; thick filament; myofibrillogenesis

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Funding

  1. NIAMS NIH HHS [AR 37344] Funding Source: Medline

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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.

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