Association of titin and myosin heavy chain in developing skeletal muscle

W. B. Isaacs, I. S. Kim, A. Struve, A. B. Fulton

Research output: Contribution to journalArticlepeer-review

27 Scopus citations


To understand molecular interactions that organize developing myofibrils, we examined the biosynthesis and interaction of titin and myosin heavy chain in cultures of developing muscle. Use of pulse-labeling, immunoprecipitation, and a reversible cross-linking procedure demonstrates that within minutes of synthesis, titin and myosin heavy chain can be chemically cross-linked into very large, detergent-resistant complexes retaining many features of intact myotubes. These complexes, predominantly of titin and myosin, occur very early in myofibrillogenesis as well as later. These data suggest that synthesis and assembly of titin and myosin are temporally and spatially coordinated in nascent myofibrils and support the hypothesis that titin molecules help to organize sarcomere formation.

Original languageEnglish (US)
Pages (from-to)7496-7500
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number16
StatePublished - 1992


  • Assembly in vivo
  • Cytoskeleton
  • Myogenesis

ASJC Scopus subject areas

  • General


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