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A biosensor-based framework to measure latent proteostasis capacity
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Number of Authors: 112018 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 9, article id 287Article in journal (Refereed) Published
Abstract [en]

The pool of quality control proteins (QC) that maintains protein-folding homeostasis (proteostasis) is dynamic but can become depleted in human disease. A challenge has been in quantitatively defining the depth of the QC pool. With a new biosensor, flow cytometrybased methods and mathematical modeling we measure the QC capacity to act as holdases and suppress biosensor aggregation. The biosensor system comprises a series of barnase kernels with differing folding stability that engage primarily with HSP70 and HSP90 family proteins. Conditions of proteostasis stimulation and stress alter QC holdase activity and aggregation rates. The method reveals the HSP70 chaperone cycle to be rate limited by HSP70 holdase activity under normal conditions, but this is overcome by increasing levels of the BAG1 nucleotide exchange factor to HSPA1A or activation of the heat shock gene cluster by HSF1 overexpression. This scheme opens new paths for biosensors of disease and proteostasis systems.

Place, publisher, year, edition, pages
2018. Vol. 9, article id 287
National Category
Biological Sciences
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URN: urn:nbn:se:su:diva-152722DOI: 10.1038/s41467-017-02562-5ISI: 000422745800022PubMedID: 29348634OAI: oai:DiVA.org:su-152722DiVA, id: diva2:1185615
Available from: 2018-02-26 Created: 2018-02-26 Last updated: 2018-02-26Bibliographically approved

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Oliveberg, Mikael
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Department of Biochemistry and Biophysics
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