Myosin as a potential redox-sensor: An in vitro study

Chiara Passarelli, Stefania Petrini, Anna Pastore, Valentina Bonetto, Patrizio Sale, Laura M. Gaeta, Giulia Tozzi, Enrico Bertini, Monica Canepari, Rosetta Rossi, Fiorella Piemonte

Research output: Contribution to journalArticlepeer-review


A balanced redox status is necessary to optimize force production in contractile apparatus, where free radicals generated by skeletal muscle are involved in some basic physiological processes like excitation-contraction coupling. Protein glutathionylation has a key role in redox regulation of proteins and signal transduction. Here we show that myosin is sensitive to in vitro glutathionylation and MALDI-TOF analysis identified three potential sites of glutathione binding, two of them locating on the myosin head. Glutathionylation of myosin has an important impact on the protein structure, as documented by the lower fluorescence quantum yield of glutathionylated myosin and its increased susceptibility to the proteolytic cleavage. Myosin function is also sensitive to glutathionylation, which modulates its ATPase activity depending on GSSG redox balance. Thus, like the phosphorylation/ dephosphorylation cycle, glutathionylation may represent a mechanism by which glutathione modulates sarcomere functions depending on the tissue redox state, and myosin may constitute a muscle redox-sensor.

Original languageEnglish
Pages (from-to)119-126
Number of pages8
JournalJournal of Muscle Research and Cell Motility
Issue number2-5
Publication statusPublished - May 2008


  • Glutathionylation
  • Myosin
  • Oxidative stress
  • Sarcomere

ASJC Scopus subject areas

  • Physiology
  • Cell Biology
  • Biochemistry


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