The central domain of UNC-45 chaperone inhibits the myosin power stroke.
The central domain of UNC-45 chaperone inhibits the myosin power stroke.
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DOI:
10.1002/2211-5463.12346
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发表时间:
2018-01
期刊:
影响因子:
2.6
通讯作者:
Oberhauser AF
中科院分区:
文献类型:
--
作者:
Bujalowski PJ;Nicholls P;Garza E;Oberhauser AF
The multidomain UNC‐45B chaperone is crucial for the proper folding and function of sarcomeric myosin. We recently found that UNC‐45B inhibits the translocation of actin by myosin. The main functions of the UCS and TPR domains are known but the role of the central domain remains obscure. Here, we show—using in vitro myosin motility and ATPase assays—that the central domain alone acts as an inhibitor of the myosin power stroke through a mechanism that allows ATP turnover. Hence, UNC‐45B is a unique chaperone in which the TPR domain recruits Hsp90; the UCS domain possesses chaperone‐like activities; and the central domain interacts with myosin and inhibits the actin translocation function of myosin. We hypothesize that the inhibitory function plays a critical role during the assembly of myofibrils under stress and during the sarcomere development process.
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影响因子:
64.5
作者:
Hoppe, T;Cassata, G;Baumeister, R
通讯作者:
Baumeister, R
影响因子:
6.8
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Hellerschmied D;Clausen T
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Bujalowski, Paul J.;Nicholls, Paul;Oberhauser, Andres F.
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Oberhauser, Andres F.
DOI:
10.1002/ar.22980
发表时间:
2014-09
影响因子:
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通讯作者:
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