Chaperone-mediated reversible inhibition of the sarcomeric myosin power stroke

Paul Nicholls, Paul J. Bujalowski, Henry F. Epstein, Darren F. Boehning, José M. Barral, Andres F. Oberhauser

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Molecular chaperones are required for successful folding and assembly of sarcomeric myosin in skeletal and cardiac muscle. Here, we show that the chaperone UNC-45B inhibits the actin translocation function of myosin. Further, we show that Hsp90, another chaperone involved in sarcomere development, allows the myosin to resume actin translocation. These previously unknown activities may play a key role in sarcomere development, preventing untimely myosin powerstrokes from disrupting the precise alignment of the sarcomere until it has formed completely.

Original languageEnglish (US)
Pages (from-to)3977-3981
Number of pages5
JournalFEBS Letters
Issue number21
StatePublished - Nov 3 2014


  • Actin-translocation
  • Chaperone
  • Hsp90
  • UNC-45

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


Dive into the research topics of 'Chaperone-mediated reversible inhibition of the sarcomeric myosin power stroke'. Together they form a unique fingerprint.

Cite this