Passive stiffness in Drosophila indirect flight muscle reduced by disrupting paramyosin phosphorylation, but not by embryonic myosin S2 hinge substitution.

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  • Additional Information
    • Source:
      Publisher: Cell Press Country of Publication: United States NLM ID: 0370626 Publication Model: Print-Electronic Cited Medium: Print ISSN: 0006-3495 (Print) Linking ISSN: 00063495 NLM ISO Abbreviation: Biophys J Subsets: MEDLINE
    • Publication Information:
      Publication: Cambridge, MA : Cell Press
      Original Publication: New York, Published by Rockefeller University Press [etc.] for the Biophysical Society.
    • Subject Terms:
      Drosophila/*physiology ; Myofibrils/*physiology ; Myosin Subfragments/*metabolism ; Tropomyosin/*metabolism; Animals ; Animals, Genetically Modified ; Drosophila/embryology ; Drosophila/genetics ; Drosophila Proteins/genetics ; Drosophila Proteins/physiology ; Flight, Animal ; Microscopy, Electron, Transmission ; Muscles/physiology ; Mutation ; Phosphorylation ; Sarcomeres/physiology
    • Abstract:
      High passive stiffness is one of the characteristic properties of the asynchronous indirect flight muscle (IFM) found in many insects like Drosophila. To evaluate the effects of two thick filament protein domains on passive sarcomeric stiffness, and to investigate their correlation with IFM function, we used microfabricated cantilevers and a high resolution imaging system to study the passive IFM myofibril stiffness of two groups of transgenic Drosophila lines. One group (hinge-switch mutants) had a portion of the endogenous S2 hinge region replaced by an embryonic version; the other group (paramyosin mutants) had one or more putative phosphorylation sites near the N-terminus of paramyosin disabled. Both transgenic groups showed severely compromised flight ability. In this study, we found no difference (compared to the control) in passive elastic modulus in the hinge-switch group, but a 15% reduction in the paramyosin mutants. All results were corroborated by muscle fiber mechanics experiments performed on the same lines. The fact that myofibril elasticity is unaffected by hinge switching implies alternative S2 hinges do not critically affect passive sarcomere stiffness. In contrast, the mechanical defects observed upon disrupting paramyosin phosphorylation sites in Drosophila suggests that paramyosin phosphorylation is important for maintaining high passive stiffness in IFM myofibrils, probably by affecting paramyosin's interaction with other sarcomeric proteins.
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    • Grant Information:
      R01 AR043396 United States AR NIAMS NIH HHS; R01 AR049425 United States AR NIAMS NIH HHS; AR43396 United States AR NIAMS NIH HHS; R01049425 United States PHS HHS
    • Accession Number:
      0 (Drosophila Proteins)
      0 (Myosin Subfragments)
      0 (Tropomyosin)
    • Publication Date:
      Date Created: 20061003 Date Completed: 20070208 Latest Revision: 20181113
    • Publication Date:
      20221213
    • Accession Number:
      PMC1779912
    • Accession Number:
      10.1529/biophysj.106.088492
    • Accession Number:
      17012313