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Protein painting reveals pervasive remodeling of conserved proteostasis machinery in response to pharmacological stimuli

View ORCID ProfileDezerae Cox, Angelique R. Ormsby, View ORCID ProfileGavin E. Reid, View ORCID ProfileDanny M. Hatters
doi: https://doi.org/10.1101/2022.05.14.491969
Dezerae Cox
1Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC 3010, Australia
2Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom
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  • For correspondence: dc597@cam.ac.uk dhatters@unimelb.edu.au
Angelique R. Ormsby
1Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC 3010, Australia
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Gavin E. Reid
1Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC 3010, Australia
3School of Chemistry, The University of Melbourne, Parkville, VIC 3010, Australia
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Danny M. Hatters
1Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC 3010, Australia
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  • For correspondence: dc597@cam.ac.uk dhatters@unimelb.edu.au
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Abstract

Accurate spatio-temporal organization of the proteome is essential for cellular homeostasis. However, a detailed mechanistic understanding of this organization and how it is altered in response to external stimuli in the intact cellular environment is as-yet unrealized. To address this need, ‘protein painting’ methods have emerged as a way to gain insight into the conformational status of proteins within cells at the proteome-wide scale. For example, tetraphenylethene maleimide (TPE-MI) has previously been used to quantify the engagement of quality control machinery with client proteins in cell lysates. Here, we showcase the ability of TPE-MI to additionally reveal proteome network remodeling in whole cells in response to a cohort of commonly used pharmacological stimuli of varying specificity. We report specific, albeit heterogeneous, responses to individual stimuli that coalesce on a conserved set of core cellular machineries. This work expands our understanding of proteome conformational remodeling in response to cellular stimuli, and provides a blueprint for assessing how these conformational changes may contribute to disorders characterized by proteostasis imbalance.

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 May 29, 2022.
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Protein painting reveals pervasive remodeling of conserved proteostasis machinery in response to pharmacological stimuli
Dezerae Cox, Angelique R. Ormsby, Gavin E. Reid, Danny M. Hatters
bioRxiv 2022.05.14.491969; doi: https://doi.org/10.1101/2022.05.14.491969
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Protein painting reveals pervasive remodeling of conserved proteostasis machinery in response to pharmacological stimuli
Dezerae Cox, Angelique R. Ormsby, Gavin E. Reid, Danny M. Hatters
bioRxiv 2022.05.14.491969; doi: https://doi.org/10.1101/2022.05.14.491969

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