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Thiol-Based Redox Signaling: Impacts on Molecular Chaperones and Cellular Proteostasis

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Book cover Heat Shock Proteins in Signaling Pathways

Part of the book series: Heat Shock Proteins ((HESP,volume 17))

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Abstract

Signaling through protein cysteine residues to regulate diverse biological processes is widely conserved from bacterial to human cells. Differential cysteine reactivity enables cells to sense and respond to perturbations in the cellular redox environment, which may impact protein structure and activity. This chapter will focus on how redox signaling regulates components of the protein quality control network to mitigate proteotoxic stress caused by redox active compounds. While specifics of redox-based activation of the endoplasmic reticulum unfolded protein response and the cytoplasmic heat shock and oxidative stress responses differ, the presence of regulatory proteins containing reactive cysteines is a common feature. Moreover, several protein chaperones are reversibly regulated via cysteine switches that govern their ability to protect or refold damaged polypeptides. These responses are biologically indispensable, given the propensity of dysregulated cells to produce endogenous reactive oxygen species and the prevalence of thiol-reactive xenobiotics in the external environment.

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Abbreviations

CRD:

cysteine-rich domain

Cys:

cysteine

ER:

endoplasmic reticulum

HMW:

high molecular weight

HS:

heat shock

HSP:

heat shock protein

HSR:

heat shock response

LMW:

low molecular weight

NBD:

nucleotide binding domain

NEF:

nucleotide exchange factor

OS:

oxidative stress

OSR:

oxidative stress response

PDI:

protein disulfide isomerase

PQC:

protein quality control

Prx:

peroxiredoxin

ROS:

reactive oxygen species

SOH:

sulfenic acid

TF:

transcription factor

Ub:

ubiquitin

UPR:

unfolded protein response

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Acknowledgements

Work in the authors’ laboratory was supported by NIH grant GM127287.

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Authors and Affiliations

  1. Department of Microbiology and Molecular Genetics, University of Texas McGovern Medical School at Houston, Houston, TX, USA

    Amy E. Ford & Kevin A. Morano

  2. MD Anderson UT Health Graduate School of Biomedical Sciences, Houston, TX, USA

    Amy E. Ford

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  1. Amy E. Ford
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  2. Kevin A. Morano
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Correspondence to Kevin A. Morano .

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Editors and Affiliations

  1. Professor, Department of Medicine and Director, Precision Therapeutics Proteogenomics Diagnostic Center Eleanor N. Dana Cancer Center, University of Toledo College of Medicine and Life Sciences, Toledo, OH, USA

    Alexzander A. A. Asea

  2. Department of Experimental Radiation Oncology, MD Anderson Cancer Center, Houston, TX, USA

    Punit Kaur

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Ford, A.E., Morano, K.A. (2019). Thiol-Based Redox Signaling: Impacts on Molecular Chaperones and Cellular Proteostasis. In: Asea, A., Kaur, P. (eds) Heat Shock Proteins in Signaling Pathways. Heat Shock Proteins, vol 17. Springer, Cham. https://doi.org/10.1007/978-3-030-03952-3_1

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