Does actin bind to the ends of thin filaments in skeletal muscle?

S. Ishiwata, T. Funatsu

    Research output: Contribution to journalArticle

    37 Citations (Scopus)

    Abstract

    We examined whether or not purified actin binds to the ends of thin filaments in rabbit skeletal myofibrils. Phase-contrast, fluorescence, and electron microscopic observations revealed that actin does not bind to the ends of thin filaments of intact myofibrils. However, in I-Z-I brushes prepared by dissolving thick filaments at high ionic strength, marked binding of actin to the free ends, i.e., the pointed ends, of thin filaments was observed when actin was added at an early phase of polymerization. As the polymerization of actin proceeded, the binding efficiency decreased. The critical actin concentration for this binding was higher than that for polymerization in solution. The binding of G-actin was not observed at low ionic strength. On the basis of these results, we suggest that a particular structure suppressing the binding of actin is present at the free ends of thin filaments in intact myofibrils and that a part of the end structure population is eliminated or modified at high ionic strength so that further binding of actin becomes possible. The myofibril and I-Z-I brush appear to be useful systems for studies aimed at elucidating the organization mechanisms of actin filaments in vivo.

    Original languageEnglish
    Pages (from-to)282-291
    Number of pages10
    JournalJournal of Cell Biology
    Volume100
    Issue number1
    Publication statusPublished - 1985

    ASJC Scopus subject areas

    • Cell Biology

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