Actin and myosin: control of filament assembly.

J. A. Spudich*, J. D. Pardee, P. A. Simpson, K. Yamamoto, E. R. Kuczmarski, L. Stryer

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

Actin filaments, assembled from highly purified actin from either skeletal muscle or Dictyostelium amoebae, are very stable under physiological ionic conditions. A small and limited amount of exchange of actin filament subunits for unpolymerized actin or subunits in other filaments has been measured by three techniques: fluorescence energy transfer, incorporation of 35S-labelled actin monomers into unlabelled actin filaments, and exchange of [14C]ATP with filament-bound ADP. A 40 kDa protein purified from amoebae destabilizes these otherwise stable filaments in a Ca2+-dependent manner. Myosin purified from Dictyostelium amoebae is phosphorylated both in the tail region of the heavy chain and in one of the light chains. Phosphorylation appears to regulate myosin thick-filament formation.

Original languageEnglish (US)
Pages (from-to)247-261
Number of pages15
JournalPhilosophical transactions of the Royal Society of London. Series B, Biological sciences
Volume299
Issue number1095
DOIs
StatePublished - Jan 1 1982

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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