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Frumkin A, Dror S, Pokrzywa W, et al. Challenging muscle homeostasis uncovers novel chaperone interactions in Caenorhabditis elegans. Front Mol Biosci. 2014;1:21doi: 10.3389/fmolb.2014.00021.
Frumkin, A., Dror, S., Pokrzywa, W., Bar-Lavan, Y., Karady, I., Hoppe, T., & Ben-Zvi, A. (2014). Challenging muscle homeostasis uncovers novel chaperone interactions in Caenorhabditis elegans. Frontiers in molecular biosciences, 121. https://doi.org/10.3389/fmolb.2014.00021
Frumkin, Anna, et al. "Challenging muscle homeostasis uncovers novel chaperone interactions in Caenorhabditis elegans." Frontiers in molecular biosciences vol. 1 (2014): 21. doi: https://doi.org/10.3389/fmolb.2014.00021
Frumkin A, Dror S, Pokrzywa W, Bar-Lavan Y, Karady I, Hoppe T, Ben-Zvi A. Challenging muscle homeostasis uncovers novel chaperone interactions in Caenorhabditis elegans. Front Mol Biosci. 2014 Nov 06;1:21. doi: 10.3389/fmolb.2014.00021. eCollection 2014. PMID: 25988162; PMCID: PMC4428482.
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Front Mol Biosci. 2014 Nov 06;1:21. doi: 10.3389/fmolb.2014.00021. eCollection 2014.

Challenging muscle homeostasis uncovers novel chaperone interactions in Caenorhabditis elegans.

Frontiers in molecular biosciences

Anna Frumkin, Shiran Dror, Wojciech Pokrzywa, Yael Bar-Lavan, Ido Karady, Thorsten Hoppe, Anat Ben-Zvi

Affiliations

  1. Department of Life Sciences and The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev Beer Sheva, Israel.
  2. Institute for Genetics and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne Cologne, Germany ; Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases, CECAD Research Center, University of Cologne Cologne, Germany.

PMID: 25988162 PMCID: PMC4428482 DOI: 10.3389/fmolb.2014.00021

Abstract

Proteome stability is central to cellular function and the lifespan of an organism. This is apparent in muscle cells, where incorrect folding and assembly of the sarcomere contributes to disease and aging. Apart from the myosin-assembly factor UNC-45, the complete network of chaperones involved in assembly and maintenance of muscle tissue is currently unknown. To identify additional factors required for sarcomere quality control, we performed genetic screens based on suppressed or synthetic motility defects in Caenorhabditis elegans. In addition to ethyl methyl sulfonate-based mutagenesis, we employed RNAi-mediated knockdown of candidate chaperones in unc-45 temperature-sensitive mutants and screened for impaired movement at permissive conditions. This approach confirmed the cooperation between UNC-45 and Hsp90. Moreover, the screens identified three novel co-chaperones, CeHop (STI-1), CeAha1 (C01G10.8) and Cep23 (ZC395.10), required for muscle integrity. The specific identification of Hsp90 and Hsp90 co-chaperones highlights the physiological role of Hsp90 in myosin folding. Our work thus provides a clear example of how a combination of mild perturbations to the proteostasis network can uncover specific quality control modules.

Keywords: Caenorhabditis elegans; DAF-21; Hsp90; UNC-45; chaperones; misfolding; myosin; proteostasis

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