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Article ; Online: Function, Therapeutic Potential, and Inhibition of Hsp70 Chaperones.

Ambrose, Andrew J / Chapman, Eli

2021 Volume 64, Issue 11, Page(s) 7060–7082

Abstract: Hsp70s are among the most highly conserved proteins in all of biology. Through an iterative binding and release of exposed hydrophobic residues on client proteins, Hsp70s can prevent aggregation and promote folding to the native state of their client ... ...

Abstract	Hsp70s are among the most highly conserved proteins in all of biology. Through an iterative binding and release of exposed hydrophobic residues on client proteins, Hsp70s can prevent aggregation and promote folding to the native state of their client proteins. The human proteome contains eight canonical Hsp70s. Because Hsp70s are relatively promiscuous they play a role in folding a large proportion of the proteome. Hsp70s are implicated in disease through their ability to regulate protein homeostasis. In recent years, researchers have attempted to develop selective inhibitors of Hsp70 isoforms to better understand the role of individual isoforms in biology and as potential therapeutics. Selective inhibitors have come from rational design, forced localization, and serendipity, but the development of completely selective inhibitors remains elusive. In the present review, we discuss the Hsp70 structure and function, the known Hsp70 client proteins, the role of Hsp70s in disease, and current efforts to discover Hsp70 modulators.
MeSH term(s)	Allosteric Regulation ; Endoplasmic Reticulum/metabolism ; HSP70 Heat-Shock Proteins/antagonists & inhibitors ; HSP70 Heat-Shock Proteins/metabolism ; Humans ; Neoplasms/metabolism ; Neoplasms/pathology ; Protein Domains ; Protein Folding ; Protein Isoforms/antagonists & inhibitors ; Protein Isoforms/metabolism ; Substrate Specificity
Chemical Substances	HSP70 Heat-Shock Proteins ; Protein Isoforms
Language	English
Publishing date	2021-05-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	218133-2
ISSN	1520-4804 ; 0022-2623
ISSN (online)	1520-4804
ISSN	0022-2623
DOI	10.1021/acs.jmedchem.0c02091
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Article ; Online: The role of natural products in revealing NRF2 function.

Zhang, Donna D / Chapman, Eli

Natural product reports

2020 Volume 37, Issue 6, Page(s) 797–826

Abstract: Covering: up to 2020The transcription factor NRF2 is one of the body's major defense mechanisms, driving transcription of >300 antioxidant response element (ARE)-regulated genes that are involved in many critical cellular processes including redox ... ...

Abstract	Covering: up to 2020The transcription factor NRF2 is one of the body's major defense mechanisms, driving transcription of >300 antioxidant response element (ARE)-regulated genes that are involved in many critical cellular processes including redox regulation, proteostasis, xenobiotic detoxification, and primary metabolism. The transcription factor NRF2 and natural products have an intimately entwined history, as the discovery of NRF2 and much of its rich biology were revealed using natural products both intentionally and unintentionally. In addition, in the last decade a more sinister aspect of NRF2 biology has been revealed. NRF2 is normally present at very low cellular levels and only activated when needed, however, it has been recently revealed that chronic, high levels of NRF2 can lead to diseases such as diabetes and cancer, and may play a role in other diseases. Again, this "dark side" of NRF2 was revealed and studied largely using a natural product, the quassinoid, brusatol. In the present review, we provide an overview of NRF2 structure and function to orient the general reader, we will discuss the history of NRF2 and NRF2-activating compounds and the biology these have revealed, and we will delve into the dark side of NRF2 and contemporary issues related to the dark side biology and the role of natural products in dissecting this biology.
MeSH term(s)	Animals ; Biological Products/chemistry ; Biological Products/pharmacology ; Flavanones/pharmacology ; Humans ; Kelch-Like ECH-Associated Protein 1/chemistry ; Kelch-Like ECH-Associated Protein 1/metabolism ; NF-E2-Related Factor 2/antagonists & inhibitors ; NF-E2-Related Factor 2/chemistry ; NF-E2-Related Factor 2/metabolism ; NF-E2-Related Factor 2/physiology ; Quassins/pharmacology
Chemical Substances	Biological Products ; Flavanones ; Kelch-Like ECH-Associated Protein 1 ; NF-E2-Related Factor 2 ; Quassins ; brusatol (14907-98-3) ; wogonin (POK93PO28W)
Language	English
Publishing date	2020-05-13
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	2002546-4
ISSN	1460-4752 ; 0265-0568
ISSN (online)	1460-4752
ISSN	0265-0568
DOI	10.1039/c9np00061e
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Anti-Ferroptotic Effects of Nrf2: Beyond the Antioxidant Response.

Shakya, Aryatara / McKee, Nicholas W / Dodson, Matthew / Chapman, Eli / Zhang, Donna D

Molecules and cells

2023 Volume 46, Issue 3, Page(s) 165–175

Abstract: The transcription factor Nrf2 was originally identified as a master regulator of redox homeostasis, as it governs the expression of a battery of genes involved in mitigating oxidative and electrophilic stress. However, the central role of Nrf2 in ... ...

Abstract	The transcription factor Nrf2 was originally identified as a master regulator of redox homeostasis, as it governs the expression of a battery of genes involved in mitigating oxidative and electrophilic stress. However, the central role of Nrf2 in dictating multiple facets of the cellular stress response has defined the Nrf2 pathway as a general mediator of cell survival. Recent studies have indicated that Nrf2 regulates the expression of genes controlling ferroptosis, an ironand lipid peroxidation-dependent form of cell death. While Nrf2 was initially thought to have anti-ferroptotic function primarily through regulation of the antioxidant response, accumulating evidence has indicated that Nrf2 also exerts anti-ferroptotic effects via regulation of key aspects of iron and lipid metabolism. In this review, we will explore the emerging role of Nrf2 in mediating iron homeostasis and lipid peroxidation, where several Nrf2 target genes have been identified that encode critical proteins involved in these pathways. A better understanding of the mechanistic relationship between Nrf2 and ferroptosis, including how genetic and/or pharmacological manipulation of Nrf2 affect the ferroptotic response, should facilitate the development of new therapies that can be used to treat ferroptosis-associated diseases.
MeSH term(s)	Antioxidants ; NF-E2-Related Factor 2/genetics ; NF-E2-Related Factor 2/metabolism ; Reactive Oxygen Species/metabolism ; Cell Death ; Iron/metabolism
Chemical Substances	Antioxidants ; NF-E2-Related Factor 2 ; Reactive Oxygen Species ; Iron (E1UOL152H7)
Language	English
Publishing date	2023-03-24
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	1148964-9
ISSN	0219-1032 ; 1016-8478
ISSN (online)	0219-1032
ISSN	1016-8478
DOI	10.14348/molcells.2023.0005
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Article ; Online: Targeting NRF2 to treat cancer.

Sivinski, Jared / Zhang, Donna D / Chapman, Eli

Seminars in cancer biology

2021 Volume 76, Page(s) 61–73

Abstract: NRF2 is a basic leucine zipper (bZip) transcription factor that is the master regulator of redox homeostasis. Under basal conditions, the cellular level of NRF2 is low due to a posttranslational regulation by the ubiquitin proteasome system (UPS). But, ... ...

Abstract	NRF2 is a basic leucine zipper (bZip) transcription factor that is the master regulator of redox homeostasis. Under basal conditions, the cellular level of NRF2 is low due to a posttranslational regulation by the ubiquitin proteasome system (UPS). But, when an organism is challenged with oxidative or xenobiotic stress, the NRF2 pathway is activated by inhibition of the E3 ubiquitin ligase complex that normally marks NRF2 for destruction. For several decades, researchers have searched for molecules that can intentionally activate NRF2, as this was shown to be a means to prevent certain diseases, at least in animal models. In the present era, there are many compounds known to activate the NRF2 pathway including natural products and synthetic compounds, covalent and non-covalent compounds, and others. However, it was also revealed that like many protective pathways, the NRF2 pathway has a dark side. Just as NRF2 can protect normal cells from damage, it can protect malignant cells from damage. As cells transform, they are exposed to many stressors and aberrant upregulation of NRF2 can facilitate transformation and it can help cancer cells to grow, to spread, and to resist treatment. For this reason, researchers are also interested in the discovery and development of NRF2 inhibitors. In the present review, we will begin with a general discussion of NRF2 structure and function, we will discuss the latest in NRF2 non-covalent activators, and we will discuss the current state of NRF2 inhibitors.
MeSH term(s)	Animals ; Humans ; Molecular Targeted Therapy/methods ; NF-E2-Related Factor 2/antagonists & inhibitors ; Neoplasms
Chemical Substances	NF-E2-Related Factor 2
Language	English
Publishing date	2021-06-05
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1033980-2
ISSN	1096-3650 ; 1044-579X
ISSN (online)	1096-3650
ISSN	1044-579X
DOI	10.1016/j.semcancer.2021.06.003
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Article: The role of natural products in revealing NRF2 function

Zhang, Donna D. / Chapman, Eli

Natural product reports. 2020 June 24, v. 37, no. 6

2020

Abstract: The transcription factor NRF2 is one of the body's major defense mechanisms, driving transcription of >300 antioxidant response element (ARE)-regulated genes that are involved in many critical cellular processes including redox regulation, proteostasis, ... ...

Abstract	The transcription factor NRF2 is one of the body's major defense mechanisms, driving transcription of >300 antioxidant response element (ARE)-regulated genes that are involved in many critical cellular processes including redox regulation, proteostasis, xenobiotic detoxification, and primary metabolism. The transcription factor NRF2 and natural products have an intimately entwined history, as the discovery of NRF2 and much of its rich biology were revealed using natural products both intentionally and unintentionally. In addition, in the last decade a more sinister aspect of NRF2 biology has been revealed. NRF2 is normally present at very low cellular levels and only activated when needed, however, it has been recently revealed that chronic, high levels of NRF2 can lead to diseases such as diabetes and cancer, and may play a role in other diseases. Again, this “dark side” of NRF2 was revealed and studied largely using a natural product, the quassinoid, brusatol. In the present review, we provide an overview of NRF2 structure and function to orient the general reader, we will discuss the history of NRF2 and NRF2-activating compounds and the biology these have revealed, and we will delve into the dark side of NRF2 and contemporary issues related to the dark side biology and the role of natural products in dissecting this biology.
Keywords	antioxidant activity ; diabetes ; metabolism ; transcription factors ; xenobiotics
Language	English
Dates of publication	2020-0624
Size	p. 797-826.
Publishing place	The Royal Society of Chemistry
Document type	Article
ZDB-ID	2002546-4
ISSN	1460-4752 ; 0265-0568
ISSN (online)	1460-4752
ISSN	0265-0568
DOI	10.1039/c9np00061e
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: eIF4A inhibition: ready for primetime?

Cunningham, Tyler A / Chapman, Eli / Schatz, Jonathan H

Oncotarget

2018 Volume 9, Issue 85, Page(s) 35515–35516

Language	English
Publishing date	2018-10-30
Publishing country	United States
Document type	Editorial
ZDB-ID	2560162-3
ISSN	1949-2553 ; 1949-2553
ISSN (online)	1949-2553
ISSN	1949-2553
DOI	10.18632/oncotarget.26268
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Article ; Online: Human Hsp70 Substrate-Binding Domains Recognize Distinct Client Proteins.

Ambrose, Andrew J / Zerio, Christopher J / Sivinski, Jared / Zhu, Xiaoyi / Godek, Jack / Sanchez, Jonathan L / Khanna, May / Khanna, Rajesh / Lairson, Luke / Zhang, Donna D / Chapman, Eli

Biochemistry

2024 Volume 63, Issue 3, Page(s) 251–263

Abstract: The 13 Hsp70 proteins in humans act on unique sets of substrates with diversity often being attributed to J-domain-containing protein (Hsp40 or JDP) cofactors. We were therefore surprised to find drastically different binding affinities for Hsp70-peptide ...

Abstract	The 13 Hsp70 proteins in humans act on unique sets of substrates with diversity often being attributed to J-domain-containing protein (Hsp40 or JDP) cofactors. We were therefore surprised to find drastically different binding affinities for Hsp70-peptide substrates, leading us to probe substrate specificity among the 8 canonical Hsp70s from humans. We used peptide arrays to characterize Hsp70 binding and then mined these data using machine learning to develop an algorithm for isoform-specific prediction of Hsp70 binding sequences. The results of this algorithm revealed recognition patterns not predicted based on local sequence alignments. We then showed that none of the human isoforms can complement heat-shocked DnaK knockout
MeSH term(s)	Humans ; Heat-Shock Proteins/metabolism ; Escherichia coli Proteins/chemistry ; Binding Sites ; HSP70 Heat-Shock Proteins/metabolism ; HSP40 Heat-Shock Proteins/metabolism ; Escherichia coli/genetics ; Escherichia coli/metabolism ; Peptides/metabolism ; Protein Binding
Chemical Substances	Heat-Shock Proteins ; Escherichia coli Proteins ; HSP70 Heat-Shock Proteins ; HSP40 Heat-Shock Proteins ; Peptides
Language	English
Publishing date	2024-01-20
Publishing country	United States
Document type	Journal Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.3c00531
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Article ; Online: Molecular Dynamics Simulations Identify Tractable Lead-like Phenyl-Piperazine Scaffolds as eIF4A1 ATP-competitive Inhibitors.

Essegian, Derek J / Cunningham, Tyler A / Zerio, Christopher J / Chapman, Eli / Schatz, Jonathan / Schürer, Stephan C

ACS omega

2021 Volume 6, Issue 38, Page(s) 24432–24443

Abstract: eIF4A1 is an ATP-dependent RNA helicase whose overexpression and activity have been tightly linked to oncogenesis in a number of malignancies. An understanding of the complex kinetics and conformational changes of this translational enzyme is necessary ... ...

Abstract	eIF4A1 is an ATP-dependent RNA helicase whose overexpression and activity have been tightly linked to oncogenesis in a number of malignancies. An understanding of the complex kinetics and conformational changes of this translational enzyme is necessary to map out all targetable binding sites and develop novel, chemically tractable inhibitors. We herein present a comprehensive quantitative analysis of eIF4A1 conformational changes using protein-ligand docking, homology modeling, and extended molecular dynamics simulations. Through this, we report the discovery of a novel, biochemically active phenyl-piperazine pharmacophore, which is predicted to target the ATP-binding site and may serve as the starting point for medicinal chemistry optimization efforts. This is the first such report of an ATP-competitive inhibitor for eiF4A1, which is predicted to bind in the nucleotide cleft. Our novel interdisciplinary pipeline serves as a framework for future drug discovery efforts for targeting eiF4A1 and other proteins with complex kinetics.
Language	English
Publishing date	2021-09-15
Publishing country	United States
Document type	Journal Article
ISSN	2470-1343
ISSN (online)	2470-1343
DOI	10.1021/acsomega.1c02805
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Article ; Online: The intricacies of NRF2 regulation in cancer.

Schmidlin, Cody J / Shakya, Aryatara / Dodson, Matthew / Chapman, Eli / Zhang, Donna D

Seminars in cancer biology

2021 Volume 76, Page(s) 110–119

Abstract: The complex role of NRF2 in the context of cancer continues to evolve. As a transcription factor, NRF2 regulates various genes involved in redox homeostasis, protein degradation, DNA repair, and xenobiotic metabolism. As such, NRF2 is critical in ... ...

Abstract	The complex role of NRF2 in the context of cancer continues to evolve. As a transcription factor, NRF2 regulates various genes involved in redox homeostasis, protein degradation, DNA repair, and xenobiotic metabolism. As such, NRF2 is critical in preserving cell function and viability, particularly during stress. Importantly, NRF2 itself is regulated via a variety of mechanisms, and the mode of NRF2 activation often dictates the duration of NRF2 signaling and its role in either preventing cancer initiation or promoting cancer progression. Herein, different modes of NRF2 regulation, including oxidative stress, autophagy dysfunction, protein-protein interactions, and epigenetics, as well as pharmacological modulators targeting this cascade in cancer, are explored. Specifically, how the timing and duration of these different mechanisms of NRF2 induction affect tumor initiation, progression, and metastasis are discussed. Additionally, progress in the discovery and development of NRF2 inhibitors for the treatment of NRF2-addicted cancers is highlighted, including modulators that inhibit specific NRF2 downstream targets. Overall, a better understanding of the intricate nature of NRF2 regulation in specific cancer contexts should facilitate the generation of novel therapeutics designed to not only prevent tumor initiation, but also halt progression and ultimately improve patient wellbeing and survival.
MeSH term(s)	Animals ; Cell Transformation, Neoplastic/metabolism ; Cell Transformation, Neoplastic/pathology ; Gene Expression Regulation, Neoplastic/physiology ; Humans ; NF-E2-Related Factor 2/metabolism ; Neoplasms/metabolism ; Neoplasms/pathology
Chemical Substances	NF-E2-Related Factor 2
Language	English
Publishing date	2021-05-18
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1033980-2
ISSN	1096-3650 ; 1044-579X
ISSN (online)	1096-3650
ISSN	1044-579X
DOI	10.1016/j.semcancer.2021.05.016
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Article ; Online: FAM129B-dependent activation of NRF2 promotes an invasive phenotype in BRAF mutant melanoma cells.

Schmidlin, Cody J / Tian, Wang / Dodson, Matthew / Chapman, Eli / Zhang, Donna D

Molecular carcinogenesis

2021 Volume 60, Issue 5, Page(s) 331–341

Abstract: Incidence of melanoma continues to rise in the United States with ~100,000 new cases diagnosed in 2019. While the 5-year survival rate of melanoma is 99% when localized, the rate of survival drops to 22.5% when distant disease is detected. As such, an ... ...

Abstract	Incidence of melanoma continues to rise in the United States with ~100,000 new cases diagnosed in 2019. While the 5-year survival rate of melanoma is 99% when localized, the rate of survival drops to 22.5% when distant disease is detected. As such, an area of great interest is understanding the mechanisms that promote melanoma metastasis so that better potential therapeutic targets can be discovered. Herein, we demonstrate that activation of NRF2 by FAM129B contributes to increased metastatic potential of BRAF V600E mutant melanoma cells. Specifically, FAM129B induces NRF2 by competing for Kelch-like ECH-associated protein 1 (KEAP1) binding (the negative regulator of NRF2) via an ETGE motif. Furthermore, we show that phosphorylation of FAM129B plays a role in mediating the interaction between FAM129B and KEAP1, as the phosphorylation status of FAM129B dictates its subcellular localization. When phosphorylated, FAM129B is found primarily in the cytosol where it can bind to KEAP1, but upon inhibition of mitogen-activated protein kinase kinase activity, FAM129B is localized to the cell membrane and no longer interacts with KEAP1. In BRAF V600E mutant melanoma, the mitogen-activated protein kinase pathway leads to hyperphosphorylation of FAM129B, and therefore FAM129B localizes to the cytosol, binds KEAP1, and upregulates NRF2. Importantly, genetic modulation or pharmacological inhibition that results in a decrease in FAM129B protein level or its phosphorylation decreases migration and invasion of mutant melanoma in an NRF2-dependent manner. Overall, these data indicate that phosphorylation of FAM129B plays a significant role in driving the metastatic potential of BRAF V600E melanoma via upregulation of the NRF2 signaling pathway.
MeSH term(s)	Binding Sites ; Cell Line, Tumor ; Cell Movement ; Cell Proliferation ; Cytosol/metabolism ; HEK293 Cells ; Humans ; Kelch-Like ECH-Associated Protein 1/metabolism ; Melanoma/genetics ; Melanoma/metabolism ; Melanoma/pathology ; Mutation ; NF-E2-Related Factor 2/chemistry ; NF-E2-Related Factor 2/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Proto-Oncogene Proteins B-raf/genetics
Chemical Substances	KEAP1 protein, human ; Kelch-Like ECH-Associated Protein 1 ; NF-E2-Related Factor 2 ; NFE2L2 protein, human ; NIBAN2 protein, human ; Phosphoproteins ; BRAF protein, human (EC 2.7.11.1) ; Proto-Oncogene Proteins B-raf (EC 2.7.11.1)
Language	English
Publishing date	2021-03-08
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1004029-8
ISSN	1098-2744 ; 0899-1987
ISSN (online)	1098-2744
ISSN	0899-1987
DOI	10.1002/mc.23295
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