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

doi:10.1016/j.febslet.2014.09.013

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 journal › Article › peer-review

9 Scopus citations

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 language	English (US)
Pages (from-to)	3977-3981
Number of pages	5
Journal	FEBS Letters
Volume	588
Issue number	21
DOIs	https://doi.org/10.1016/j.febslet.2014.09.013
State	Published - Nov 3 2014
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2014.09.013

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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.",

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AU - Nicholls, Paul

AU - Bujalowski, Paul J.

AU - Epstein, Henry F.

AU - Boehning, Darren F.

AU - Barral, José M.

AU - Oberhauser, Andres F.

PY - 2014/11/3

Y1 - 2014/11/3

N2 - 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.

AB - 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.

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JO - FEBS Letters

JF - FEBS Letters

IS - 21

ER -

Chaperone-mediated reversible inhibition of the sarcomeric myosin power stroke

Abstract

All Science Journal Classification (ASJC) codes

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