Phosphorylation and actin activation of brain myosin.

B. Barylko, A. Sobieszek

Research output: Contribution to journalArticlepeer-review

18 Scopus citations

Abstract

A method is described for obtaining brain myosin that shows significant actin activation, after phosphorylation with chicken gizzard myosin light chain kinase. Myosin with this activity could be obtained only via the initial purification of brain actomyosin. The latter complex, isolated by a method similar to that used for smooth muscle, contained actin, myosin, tropomyosin of the non-muscle type and another actin-binding protein of approximately 100,000 daltons. From the presence of a specific myosin light chain kinase and phosphatase in brain tissue it is suggested that the regulation of actin-myosin interaction operates via phosphorylation and dephosphorylation of myosin.

Original languageEnglish (US)
Pages (from-to)369-374
Number of pages6
JournalThe EMBO journal
Volume2
Issue number3
DOIs
StatePublished - 1983

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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