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Beyond Chaperoning: UCS Proteins Emerge as Regulators of Myosin-Mediated Cellular Processes

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The Networking of Chaperones by Co-Chaperones

Part of the book series: Subcellular Biochemistry ((SCBI,volume 101))

Abstract

The UCS (UNC-45/CRO1/She4p) family of proteins has emerged as chaperones specific for the folding, assembly, and function of myosin. UCS proteins participate in various myosin-dependent cellular processes including myofibril organization and muscle functions, cell differentiation, striated muscle development, cytokinesis, and endocytosis. Mutations in the genes that code for UCS proteins cause serious defects in myosin-dependent cellular processes. UCS proteins that contain an N-terminal tetratricopeptide repeat (TPR) domain are called UNC-45. Vertebrates usually possess two variants of UNC-45, the ubiquitous general-cell UNC-45 (UNC-45A) and the striated muscle UNC-45 (UNC-45B), which is exclusively expressed in skeletal and cardiac muscles. Except for the TPR domain in UNC-45, UCS proteins comprise of several irregular armadillo (ARM) repeats that are organized into a central domain, a neck region, and the canonical C-terminal UCS domain that functions as the chaperoning module. With or without TPR, UCS proteins form linear oligomers that serve as scaffolds that mediate myosin folding, organization into myofibrils, repair, and motility. This chapter reviews emerging functions of these proteins with a focus on UNC-45 as a dedicated chaperone for folding, assembly, and function of myosin at protein and potentially gene levels. Recent experimental evidences strongly support UNC-45 as an absolute regulator of myosin, with each domain of the chaperone playing different but complementary roles during the folding, assembly, and function of myosin, as well as recruiting Hsp90 as a co-chaperone to optimize key steps. It is becoming increasingly clear that UNC-45 also regulates the transcription of several genes involved in myosin-dependent cellular processes.

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Acknowledgments

The authors are grateful to Drs. Hellerschmied and Clausen for providing the original copies of Fig. 7.2 (without the insert) and 3. Texts and figures from the second edition of this book were used with permission from Springer Nature: The Networking of Chaperones by Co-chaperones, UCS Proteins: Chaperones for Myosin and Co-chaperone for Hsp90, 2015, pages 133–152, Weiming Ni and Odutayo O. Odunuga. A. Oberhauser acknowledges support from the National Institutes of Health, grant R01GM118534.

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Authors and Affiliations

  1. Department of Chemistry and Biochemistry, Stephen F. Austin State University, Nacogdoches, TX, USA

    Odutayo O. Odunuga

  2. Department of Neuroscience, Cell Biology, & Anatomy, The University of Texas Medical Branch, Galveston, TX, USA

    Andres F. Oberhauser

Authors
  1. Odutayo O. Odunuga
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  2. Andres F. Oberhauser
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Correspondence to Odutayo O. Odunuga or Andres F. Oberhauser .

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Editors and Affiliations

  1. Biomedical Biotechnology Research Unit, Department of Biochemistry and Microbiology, Rhodes University, Grahamstown, South Africa

    Adrienne L. Edkins

  2. Faculty of Health Sciences, Higher Colleges of Technology, Sharjah, United Arab Emirates

    Gregory L. Blatch

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© 2023 The Author(s), under exclusive license to Springer Nature Switzerland AG

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Odunuga, O.O., Oberhauser, A.F. (2023). Beyond Chaperoning: UCS Proteins Emerge as Regulators of Myosin-Mediated Cellular Processes. In: Edkins, A.L., Blatch, G.L. (eds) The Networking of Chaperones by Co-Chaperones. Subcellular Biochemistry, vol 101. Springer, Cham. https://doi.org/10.1007/978-3-031-14740-1_7

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