Ca2+-calmodulin-dependent regulation of F-actin, myelin basic protein interaction

B. Barylko, Z. Dobrowolski

Research output: Contribution to journalArticlepeer-review

44 Scopus citations

Abstract

Myelin basic proteins (MBP) interacts with F-actin resulting in the precipitation of a complex of both proteins. Electron microscope observations of this complex reveal the presence of ordered bundles of F-actin filaments similar to those obtained from F-actin and troponin I. In addition to the bundles, there also appear short fragments of F-actin filaments. In the presence of CA2+ calmodulin causes a release of MBP from its complex with F-actin, accompanied by dissociation of F-actin bundles into separate filaments. Parallel to the binding of MBP to F-actin the ATPase activity of actomyosin is progressively reduced. This inhibition is reversed by calmodulin but only in the presence of Ca2+. Studies of the binding of S-1 to F-actin and to the F-actin-MBP complex indicate that the interaction sites for MBP and S-1 on the actin molecule are different.

Original languageEnglish (US)
Pages (from-to)327-335
Number of pages9
JournalEuropean Journal of Cell Biology
Volume35
Issue number2
StatePublished - Jan 1 1984

ASJC Scopus subject areas

  • Pathology and Forensic Medicine
  • Histology
  • Cell Biology

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