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Derlin Dfm1 Employs a Chaperone Function to Resolve Misfolded Membrane Protein Stress

View ORCID ProfileRachel Kandel, Jasmine Jung, Della Syau, Tiffany Kuo, View ORCID ProfileLivia Songster, View ORCID ProfileAnaline Aguayo, View ORCID ProfileSascha Duttke, View ORCID ProfileChristopher Benner, View ORCID ProfileSonya Neal
doi: https://doi.org/10.1101/2022.01.25.477788
Rachel Kandel
1Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093
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  • ORCID record for Rachel Kandel
Jasmine Jung
1Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093
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Della Syau
1Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093
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Tiffany Kuo
1Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093
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Livia Songster
1Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093
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Analine Aguayo
1Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093
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Sascha Duttke
2Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093
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Christopher Benner
2Department of Cellular and Molecular Medicine, University of California San Diego, La Jolla, CA 92093
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Sonya Neal
1Division of Biological Sciences, the Section of Cell and Developmental Biology, University of California San Diego, La Jolla, CA 92093
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  • For correspondence: seneal@ucsd.edu
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SUMMARY

Accumulation of misfolded proteins is a known source of cellular stress and can be detrimental to cellular health. While protein aggregation is a known hallmark of many diseases, the mechanisms by which protein aggregates cause toxicity and the molecular machines that prevent this toxicity are not completely understood. Here, we show that the accumulated misfolded membrane proteins form endoplasmic reticulum (ER) localized aggregates, impacting ubiquitin and proteasome homeostasis. Additionally, we have identified a chaperone ability of the yeast rhomboid pseudoprotease Dfm1 to influence solubilization of misfolded membrane proteins and prevent toxicity from misfolded membrane proteins. We establish that this function of Dfm1 does not require recruitment of the ATPase Cdc48 and it is distinct from Dfm1’s previously identified function in dislocating misfolded membrane proteins to the cytosol for degradation.

Competing Interest Statement

The authors have declared no competing interest.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted January 26, 2022.
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Derlin Dfm1 Employs a Chaperone Function to Resolve Misfolded Membrane Protein Stress
Rachel Kandel, Jasmine Jung, Della Syau, Tiffany Kuo, Livia Songster, Analine Aguayo, Sascha Duttke, Christopher Benner, Sonya Neal
bioRxiv 2022.01.25.477788; doi: https://doi.org/10.1101/2022.01.25.477788
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Derlin Dfm1 Employs a Chaperone Function to Resolve Misfolded Membrane Protein Stress
Rachel Kandel, Jasmine Jung, Della Syau, Tiffany Kuo, Livia Songster, Analine Aguayo, Sascha Duttke, Christopher Benner, Sonya Neal
bioRxiv 2022.01.25.477788; doi: https://doi.org/10.1101/2022.01.25.477788

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