Chaperone-mediated reversible inhibition of the sarcomeric myosin power stroke

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

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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
Volume588
Issue number21
DOIs
StatePublished - Nov 3 2014

Fingerprint

Sarcomeres
Myosins
Stroke
Actins
Skeletal Muscle Myosins
Cardiac Myosins
Molecular Chaperones
Muscle

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology
  • Medicine(all)

Cite this

Chaperone-mediated reversible inhibition of the sarcomeric myosin power stroke. / Nicholls, Paul; Bujalowski, Pawel; Epstein, Henry F.; Boehning, Darren F.; Barral, José M.; Oberhauser, Andres.

In: FEBS Letters, Vol. 588, No. 21, 03.11.2014, p. 3977-3981.

Research output: Contribution to journalArticle

Nicholls, Paul ; Bujalowski, Pawel ; Epstein, Henry F. ; Boehning, Darren F. ; Barral, José M. ; Oberhauser, Andres. / Chaperone-mediated reversible inhibition of the sarcomeric myosin power stroke. In: FEBS Letters. 2014 ; Vol. 588, No. 21. pp. 3977-3981.
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