Myosin Assembly, Maintenance and Degradation in Muscle: Role of the Chaperone UNC-45 in Myosin Thick Filament Dynamics
Myofibrillogenesis in striated muscle cells requires a precise ordered pathway to assemble different proteins into a linear array of sarcomeres. The sarcomere relies on interdigitated thick and thin filaments to ensure muscle contraction, as well as properly folded and catalytically active myosin he...
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doaj-6658a27947914eaead74ff622068a5962020-11-24T23:57:59ZengMDPI AGInternational Journal of Molecular Sciences1422-00672008-09-01991863187510.3390/ijms9091863Myosin Assembly, Maintenance and Degradation in Muscle: Role of the Chaperone UNC-45 in Myosin Thick Filament DynamicsDavid B. PilgrimTorah M. KachurMyofibrillogenesis in striated muscle cells requires a precise ordered pathway to assemble different proteins into a linear array of sarcomeres. The sarcomere relies on interdigitated thick and thin filaments to ensure muscle contraction, as well as properly folded and catalytically active myosin head. Achieving this organization requires a series of protein folding and assembly steps. The folding of the myosin head domain requires chaperone activity to attain its functional conformation. Folded or unfolded myosin can spontaneously assemble into short myosin filaments, but further assembly requires the short and incomplete myosin filaments to assemble into the developing thick filament. These longer filaments are then incorporated into the developing sarcomere of the muscle. Both myosin folding and assembly require factors to coordinate the formation of the thick filament in the sarcomere and these factors include chaperone molecules. Myosin folding and sarcomeric assembly requires association of classical chaperones as well as folding cofactors such as UNC-45. Recent research has suggested that UNC-45 is required beyond initial myosin head folding and may be directly or indirectly involved in different stages of myosin thick filament assembly, maintenance and degradation.http://www.mdpi.com/1422-0067/9/9/1863/Myosinchaperoneprotein foldingUNC-45motor domainheat shock protein |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
David B. Pilgrim Torah M. Kachur |
spellingShingle |
David B. Pilgrim Torah M. Kachur Myosin Assembly, Maintenance and Degradation in Muscle: Role of the Chaperone UNC-45 in Myosin Thick Filament Dynamics International Journal of Molecular Sciences Myosin chaperone protein folding UNC-45 motor domain heat shock protein |
author_facet |
David B. Pilgrim Torah M. Kachur |
author_sort |
David B. Pilgrim |
title |
Myosin Assembly, Maintenance and Degradation in Muscle: Role of the Chaperone UNC-45 in Myosin Thick Filament Dynamics |
title_short |
Myosin Assembly, Maintenance and Degradation in Muscle: Role of the Chaperone UNC-45 in Myosin Thick Filament Dynamics |
title_full |
Myosin Assembly, Maintenance and Degradation in Muscle: Role of the Chaperone UNC-45 in Myosin Thick Filament Dynamics |
title_fullStr |
Myosin Assembly, Maintenance and Degradation in Muscle: Role of the Chaperone UNC-45 in Myosin Thick Filament Dynamics |
title_full_unstemmed |
Myosin Assembly, Maintenance and Degradation in Muscle: Role of the Chaperone UNC-45 in Myosin Thick Filament Dynamics |
title_sort |
myosin assembly, maintenance and degradation in muscle: role of the chaperone unc-45 in myosin thick filament dynamics |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1422-0067 |
publishDate |
2008-09-01 |
description |
Myofibrillogenesis in striated muscle cells requires a precise ordered pathway to assemble different proteins into a linear array of sarcomeres. The sarcomere relies on interdigitated thick and thin filaments to ensure muscle contraction, as well as properly folded and catalytically active myosin head. Achieving this organization requires a series of protein folding and assembly steps. The folding of the myosin head domain requires chaperone activity to attain its functional conformation. Folded or unfolded myosin can spontaneously assemble into short myosin filaments, but further assembly requires the short and incomplete myosin filaments to assemble into the developing thick filament. These longer filaments are then incorporated into the developing sarcomere of the muscle. Both myosin folding and assembly require factors to coordinate the formation of the thick filament in the sarcomere and these factors include chaperone molecules. Myosin folding and sarcomeric assembly requires association of classical chaperones as well as folding cofactors such as UNC-45. Recent research has suggested that UNC-45 is required beyond initial myosin head folding and may be directly or indirectly involved in different stages of myosin thick filament assembly, maintenance and degradation. |
topic |
Myosin chaperone protein folding UNC-45 motor domain heat shock protein |
url |
http://www.mdpi.com/1422-0067/9/9/1863/ |
work_keys_str_mv |
AT davidbpilgrim myosinassemblymaintenanceanddegradationinmuscleroleofthechaperoneunc45inmyosinthickfilamentdynamics AT torahmkachur myosinassemblymaintenanceanddegradationinmuscleroleofthechaperoneunc45inmyosinthickfilamentdynamics |
_version_ |
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