Alteration in crossbridge kinetics caused by mutations in actin

Douglas R. Drummond, Michelle Peckham, John C. Sparrow, David C.S. White

Research output: Contribution to journalArticlepeer-review

48 Citations (Scopus)


THE generation of force during muscle contraction results from the interaction of myosin and actin. The kinetics of this force generation vary between different muscle types and within the same muscle type in different species1-2. Most attention has focused on the role of myosin isoforms in determining these differences3-5. The role of actin isoforms has received little attention, largely because of the lack of a suitable cell type in which the myosin isoform remains constant yet the actin isoforms vary. An alternative approach would be to examine the effect of actin mutations, however, most of these cause such gross disruption of muscle structure that mechanical measurements are impossible6-10. We have now identified two actin mutations which, despite involving conserved amino acids, can assemble into virtually normal myofibrils11. These amino-acid changes in actin significantly affect the kinetics of force generation by muscle fibres. One of the mutations is not in the putative myosin-binding site, demonstrating the importance of long-range effects of amino acids on actin function.

Original languageEnglish
Pages (from-to)440-442
Number of pages3
Issue number6300
Publication statusPublished - 1990
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General


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