Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin

  title={Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin},
  author={Doris Hellerschmied and Anita Lehner and Nina Frani{\vc}evi{\'c} and Renato Arnese and Chloe A Johnson and Antonia Vogel and Anton Meinhart and Robert Kurzbauer and Luiza Deszcz and Linn Gazda and Michael A. Geeves and Tim Clausen},
  journal={Nature Communications},
Myosin is a motor protein that is essential for a variety of processes ranging from intracellular transport to muscle contraction. Folding and assembly of myosin relies on a specific chaperone, UNC-45. To address its substrate-targeting mechanism, we reconstitute the interplay between Caenorhabditis elegans UNC-45 and muscle myosin MHC-B in insect cells. In addition to providing a cellular chaperone assay, the established system enabled us to produce large amounts of functional muscle myosin… 

UNC-45 assisted myosin folding depends on a conserved FX3HY motif implicated in Freeman Sheldon Syndrome

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Unc45 Activates Hsp90-dependent Folding of the Myosin Motor Domain*

This analysis of vertebrate Unc45 isoforms clearly demonstrates a direct role for Unc45 in Hsp90-mediated myosin motor domain folding and highlights major differences between the isoforms in substrate specificity and mechanism.

Role of the Myosin Assembly Protein UNC-45 as a Molecular Chaperone for Myosin

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Unc45b Forms a Cytosolic Complex with Hsp90 and Targets the Unfolded Myosin Motor Domain

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