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Lessons Learned from Two Decades of Modeling the Heat-Shock Response

The Heat Shock Response (HSR) is a highly conserved genetic system charged with protecting the proteome in a wide range of organisms and species. Experiments since the early 1980s have elucidated key elements in these pathways and revealed a canonical mode of regulation, which relies on a titration...

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Autores principales: Ranawade, Ayush, Sharma, Rati, Levine, Erel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9687914/
https://www.ncbi.nlm.nih.gov/pubmed/36358995
http://dx.doi.org/10.3390/biom12111645
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author Ranawade, Ayush
Sharma, Rati
Levine, Erel
author_facet Ranawade, Ayush
Sharma, Rati
Levine, Erel
author_sort Ranawade, Ayush
collection PubMed
description The Heat Shock Response (HSR) is a highly conserved genetic system charged with protecting the proteome in a wide range of organisms and species. Experiments since the early 1980s have elucidated key elements in these pathways and revealed a canonical mode of regulation, which relies on a titration feedback. This system has been subject to substantial modeling work, addressing questions about resilience, design and control. The compact core regulatory circuit, as well as its apparent conservation, make this system an ideal ‘hydrogen atom’ model for the regulation of stress response. Here we take a broad view of the models of the HSR, focusing on the different questions asked and the approaches taken. After 20 years of modeling work, we ask what lessons had been learned that would have been hard to discover without mathematical models. We find that while existing models lay strong foundations, many important questions that can benefit from quantitative modeling are still awaiting investigation.
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spelling pubmed-96879142022-11-25 Lessons Learned from Two Decades of Modeling the Heat-Shock Response Ranawade, Ayush Sharma, Rati Levine, Erel Biomolecules Review The Heat Shock Response (HSR) is a highly conserved genetic system charged with protecting the proteome in a wide range of organisms and species. Experiments since the early 1980s have elucidated key elements in these pathways and revealed a canonical mode of regulation, which relies on a titration feedback. This system has been subject to substantial modeling work, addressing questions about resilience, design and control. The compact core regulatory circuit, as well as its apparent conservation, make this system an ideal ‘hydrogen atom’ model for the regulation of stress response. Here we take a broad view of the models of the HSR, focusing on the different questions asked and the approaches taken. After 20 years of modeling work, we ask what lessons had been learned that would have been hard to discover without mathematical models. We find that while existing models lay strong foundations, many important questions that can benefit from quantitative modeling are still awaiting investigation. MDPI 2022-11-07 /pmc/articles/PMC9687914/ /pubmed/36358995 http://dx.doi.org/10.3390/biom12111645 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Ranawade, Ayush
Sharma, Rati
Levine, Erel
Lessons Learned from Two Decades of Modeling the Heat-Shock Response
title Lessons Learned from Two Decades of Modeling the Heat-Shock Response
title_full Lessons Learned from Two Decades of Modeling the Heat-Shock Response
title_fullStr Lessons Learned from Two Decades of Modeling the Heat-Shock Response
title_full_unstemmed Lessons Learned from Two Decades of Modeling the Heat-Shock Response
title_short Lessons Learned from Two Decades of Modeling the Heat-Shock Response
title_sort lessons learned from two decades of modeling the heat-shock response
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9687914/
https://www.ncbi.nlm.nih.gov/pubmed/36358995
http://dx.doi.org/10.3390/biom12111645
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