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A small-molecule inhibitor of skeletal muscle myosin II

Nature Cell Biology, ISSN: 1465-7392, Vol: 4, Issue: 1, Page: 83-88
2002
  • 238
    Citations
  • 0
    Usage
  • 189
    Captures
  • 1
    Mentions
  • 0
    Social Media
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  • Citations
    238
  • Captures
    189
  • Mentions
    1
    • References
      1
      • Wikipedia
        1

Article Description

We screened a small-molecule library for inhibitors of rabbit muscle myosin II subfragment 1 (S1) actin-stimulated ATPase activity. The best inhibitor, N-benzyl-p-toluene sulphonamide (BTS), an aryl sulphonamide, inhibited the Ca-stimulated S1 ATPase, and reversibly blocked gliding motility. Although BTS does not compete for the nucleotide-binding site of myosin, it weakens myosin's interaction with F-actin. BTS reversibly suppressed force production in skinned skeletal muscle fibres from rabbit and frog skin at micromolar concentrations. BTS suppressed twitch production of intact frog fibres with minimum alteration of Ca metabolism. BTS is remarkably specific, as it was much less effective in suppressing contraction in rat myocardial or rabbit slow-twitch muscle, and did not inhibit platelet myosin II. The isolation of BTS and the recently discovered Eg5 kinesin inhibitor, monastrol, suggests that motor proteins may be potential targets for therapeutic applications.

Bibliographic Details

A. Cheung; T. J. Mitchinson; A. F. Straight; J. A. Dantzig; S. Hollingworth; S. M. Baylor; Y. E. Goldman

Springer Science and Business Media LLC

Biochemistry, Genetics and Molecular Biology

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