Key result
Recent structure-function studies reveal structural differences between TPR-containing and TPR-less UCS chaperones that reflect their specialized and versatile working mechanisms.
This review highlights the structural diversity and specialized mechanisms of myosin-directed UCS chaperones essential for motor protein function.
May inform myosin-related cardiac disorders; leaves open therapeutic targeting pending functional studies.
The folding and assembly of myosin motor proteins is essential for most movement processes at the cellular, but also at the organism level. Importantly, myosins, which represent a very diverse family of proteins, require the activity of general and specialized folding factors to develop their full motor function. The activities of the myosin-specific UCS (UNC-45/Cro1/She4) chaperones range from assisting acto-myosin dependent transport processes to scaffolding multi-subunit chaperone complexes, which are required to assemble myofilaments. Recent structure-function studies revealed the structural organization of TPR (tetratricopeptide repeat)-containing and TPR-less UCS chaperones. The observed structural differences seem to reflect the specialized and remarkably versatile working mechanisms of myosin-directed chaperones, as will be discussed in this review.
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Hellerschmied et al. (2013) conducted a review in Myosin motor protein folding and assembly. Myosin chaperones was evaluated. Recent structure-function studies reveal structural differences between TPR-containing and TPR-less UCS chaperones that reflect their specialized and versatile working mechanisms.
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