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Background  Mutations in myosin chaperones Unc45b and Hsp90aa1.1 as well as in the Unc45b-binding protein Smyd1b impair formation of myofibrils in skeletal muscle and lead to the accumulation of misfolded myosin. The concomitant transcriptional response involves up-regulation of the three genes encoding these proteins, as well as genes involved in muscle development. The transcriptional up-regulation of  unc45b ,  hsp90aa1.1  and  smyd1b  is specific to zebrafish mutants with myosin folding defects, and is not triggered in other zebrafish myopathy models.    Results  By dissecting the promoter of  unc45b , we identify a Heat shock factor 1 (Hsf1) binding element as a mediator of  unc45b  up-regulation in myofibers lacking myosin folding proteins. Loss-of-function of Hsf1 abolishes  unc45b  up-regulation in mutants with defects in myosin folding.    Conclusions  Taken together, our data show that skeletal muscle cells respond to defective myosin chaperones with a complex gene program and suggest that this response is mediated by Hsf1 activation.    Electronic supplementary material  The online version of this article (doi:10.1186/s13059-015-0825-8) contains supplementary material, which is available to authorized users.

Loss of function of myosin chaperones triggers Hsf1-mediated transcriptional response in skeletal muscle cells