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Article ; Online: Immunoproteasome-specific subunit PSMB9 induction is required to regulate cellular proteostasis upon mitochondrial dysfunction.

Kim, Minji / Serwa, Remigiusz A / Samluk, Lukasz / Suppanz, Ida / Kodroń, Agata / Stępkowski, Tomasz M / Elancheliyan, Praveenraj / Tsegaye, Biniyam / Oeljeklaus, Silke / Wasilewski, Michal / Warscheid, Bettina / Chacinska, Agnieszka

Nature communications

2023 Volume 14, Issue 1, Page(s) 4092

Abstract: Perturbed cellular protein homeostasis (proteostasis) and mitochondrial dysfunction play an important role in neurodegenerative diseases, however, the interplay between these two phenomena remains unclear. Mitochondrial dysfunction leads to a delay in ... ...

Abstract	Perturbed cellular protein homeostasis (proteostasis) and mitochondrial dysfunction play an important role in neurodegenerative diseases, however, the interplay between these two phenomena remains unclear. Mitochondrial dysfunction leads to a delay in mitochondrial protein import, causing accumulation of non-imported mitochondrial proteins in the cytosol and challenging proteostasis. Cells respond by increasing proteasome activity and molecular chaperones in yeast and C. elegans. Here, we demonstrate that in human cells mitochondrial dysfunction leads to the upregulation of a chaperone HSPB1 and, interestingly, an immunoproteasome-specific subunit PSMB9. Moreover, PSMB9 expression is dependent on the translation elongation factor EEF1A2. These mechanisms constitute a defense response to preserve cellular proteostasis under mitochondrial stress. Our findings define a mode of proteasomal activation through the change in proteasome composition driven by EEF1A2 and its spatial regulation, and are useful to formulate therapies to prevent neurodegenerative diseases.
MeSH term(s)	Humans ; Cytoplasm ; Mitochondria ; Peptide Elongation Factor 1 ; Proteasome Endopeptidase Complex ; Proteostasis ; Cysteine Endopeptidases/metabolism
Chemical Substances	EEF1A2 protein, human ; Peptide Elongation Factor 1 ; Proteasome Endopeptidase Complex (EC 3.4.25.1) ; LMP-2 protein (144416-78-4) ; Cysteine Endopeptidases (EC 3.4.22.-)
Language	English
Publishing date	2023-07-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-39642-8
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Article ; Online: mitoLUHMES: An Engineered Neuronal Cell Line for the Analysis of the Motility of Mitochondria.

Stępkowski, Tomasz M / Męczyńska-Wielgosz, Sylwia / Kruszewski, Marcin

Cellular and molecular neurobiology

2017 Volume 37, Issue 6, Page(s) 1055–1066

Abstract: Perturbations in the transport of mitochondria and their quality control in neuronal cells underlie many types of neurological pathologies, whereas systems enabling convenient analysis of mitochondria behavior in cellular models of neurodegenerative ... ...

Abstract	Perturbations in the transport of mitochondria and their quality control in neuronal cells underlie many types of neurological pathologies, whereas systems enabling convenient analysis of mitochondria behavior in cellular models of neurodegenerative diseases are limited. In this study, we present a modified version of lund human mesencephalic cells, mitoLUHMES, expressing GFP and mitochondrially targeted DsRed2 fluorescent proteins, intended for in vitro analysis of mitochondria trafficking by real-time fluorescence microscopy. This cell line can be easily differentiated into neuronal phenotype and allows us to observe movements of single mitochondria in single cells grown in high-density cultures. We quantified the perturbations in mitochondria morphology and dynamics in cells treated with model neurotoxins: carbonyl cyanide m-chlorophenylhydrazone and 6-hydroxydopamine. For the first time we filmed the processes of fission, fusion, pausing, and reversal of mitochondria movement direction in LUHMES cells. We present a detailed analysis of mitochondria length, velocity, and frequency of movement for static, anterograde, and retrograde motile mitochondria. The observed neurotoxin treatment-mediated decreases in morphological and kinetic parameters of mitochondria provide foundation for the future studies exploiting mitoLUHMES as a new model for neurobiology.
Language	English
Publishing date	2017-08
Publishing country	United States
Document type	Journal Article
ZDB-ID	283404-2
ISSN	1573-6830 ; 0272-4340
ISSN (online)	1573-6830
ISSN	0272-4340
DOI	10.1007/s10571-016-0438-0
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Zs.A 1727: Show issues

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Article: The Impact of Ag Nanoparticles and CdTe Quantum Dots on Expression and Function of Receptors Involved in Amyloid-β Uptake by BV-2 Microglial Cells.

Sikorska, Katarzyna / Grądzka, Iwona / Wasyk, Iwona / Brzóska, Kamil / Stępkowski, Tomasz M / Czerwińska, Malwina / Kruszewski, Marcin K

Materials (Basel, Switzerland)

2020 Volume 13, Issue 14

Abstract: Microglial cells clear the brain of pathogens and harmful debris, including amyloid-β (Aβ) deposits that are formed during Alzheimer's disease (AD). We studied the expression of Msr1, Ager and Cd36 receptors involved in Aβ uptake and expression of Cd33 ... ...

Abstract	Microglial cells clear the brain of pathogens and harmful debris, including amyloid-β (Aβ) deposits that are formed during Alzheimer's disease (AD). We studied the expression of Msr1, Ager and Cd36 receptors involved in Aβ uptake and expression of Cd33 protein, which is considered a risk factor in AD. The effect of silver nanoparticles (AgNPs) and cadmium telluride quantum dots (CdTeQDs) on the expression of the above receptors and Aβ uptake by microglial cells was investigated. Absorption of Aβ and NPs was confirmed by confocal microscopy. AgNPs, but not CdTeQDs, caused a decrease in Aβ accumulation. By using a specific inhibitor-polyinosinic acid-we demonstrated that Aβ and AgNPs compete for scavenger receptors. Real-time PCR showed up-regulation of
Language	English
Publishing date	2020-07-20
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2487261-1
ISSN	1996-1944
ISSN	1996-1944
DOI	10.3390/ma13143227
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Article ; Online: Molecular cross-talk between the NRF2/KEAP1 signaling pathway, autophagy, and apoptosis.

Stępkowski, Tomasz M / Kruszewski, Marcin K

Free radical biology & medicine

2011 Volume 50, Issue 9, Page(s) 1186–1195

Abstract: Oxidative stress, perturbations in the cellular thiol level and redox balance, affects many cellular functions, including signaling pathways. This, in turn, may cause the induction of autophagy or apoptosis. The NRF2/KEAP1 signaling pathway is the main ... ...

Abstract	Oxidative stress, perturbations in the cellular thiol level and redox balance, affects many cellular functions, including signaling pathways. This, in turn, may cause the induction of autophagy or apoptosis. The NRF2/KEAP1 signaling pathway is the main pathway responsible for cell defense against oxidative stress and maintaining the cellular redox balance at physiological levels. The relation between NRF2/KEAP1 signaling and regulation of apoptosis and autophagy is not well understood. In this hypothesis article we discuss how KEAP1 protein and its direct interactants (such as PGAM5, prothymosin α, FAC1 (BPTF), and p62) provide a molecular foundation for a possible cross-talk between NRF2/KEAP1, apoptosis, and autophagy pathways. We present a hypothesis for how NRF2/KEAP1 may interfere with the cellular apoptosis-regulatory machinery through activation of the ASK1 kinase by a KEAP1 binding partner-PGAM5. Based on very recent experimental evidence, new hypotheses for a cross-talk between NF-κB and the NRF2/KEAP1 pathway in the context of autophagy-related "molecular hub" protein p62 are also presented. The roles of KEAP1 molecular binding partners in apoptosis regulation during carcinogenesis and in neurodegenerative diseases are also discussed.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Amino Acid Motifs ; Animals ; Antigens, Nuclear/genetics ; Antigens, Nuclear/metabolism ; Apoptosis ; Autophagy ; Carrier Proteins/genetics ; Carrier Proteins/metabolism ; Cell Transformation, Neoplastic/genetics ; Cell Transformation, Neoplastic/metabolism ; Cell Transformation, Neoplastic/pathology ; Gene Expression Regulation ; Humans ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Kelch-Like ECH-Associated Protein 1 ; MAP Kinase Kinase Kinase 5/genetics ; MAP Kinase Kinase Kinase 5/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; NF-E2-Related Factor 2/genetics ; NF-E2-Related Factor 2/metabolism ; NF-kappa B/genetics ; NF-kappa B/metabolism ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Oxidation-Reduction ; Oxidative Stress ; Phosphoprotein Phosphatases ; Phosphorylation ; Protein Binding ; Protein Precursors/genetics ; Protein Precursors/metabolism ; Reactive Oxygen Species/metabolism ; Sequestosome-1 Protein ; Signal Transduction/physiology ; Sulfhydryl Compounds/metabolism ; Thymosin/analogs & derivatives ; Thymosin/genetics ; Thymosin/metabolism ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Ubiquitination
Chemical Substances	Adaptor Proteins, Signal Transducing ; Antigens, Nuclear ; Carrier Proteins ; Intracellular Signaling Peptides and Proteins ; KEAP1 protein, human ; Kelch-Like ECH-Associated Protein 1 ; Mitochondrial Proteins ; NF-E2-Related Factor 2 ; NF-kappa B ; Nerve Tissue Proteins ; Protein Precursors ; Reactive Oxygen Species ; SQSTM1 protein, human ; Sequestosome-1 Protein ; Sulfhydryl Compounds ; Transcription Factors ; fetal Alzheimer antigen ; prothymosin alpha ; Thymosin (61512-21-8) ; MAP Kinase Kinase Kinase 5 (EC 2.7.11.25) ; PGAM5 protein, human (EC 3.1.3.16) ; Phosphoprotein Phosphatases (EC 3.1.3.16)
Language	English
Publishing date	2011-05-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2011.01.033
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Zs.A 2109: Show issues

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Article ; Online: Basal PIR expression in HeLa cells is driven by NRF2 via evolutionary conserved antioxidant response element.

Brzóska, Kamil / Stępkowski, Tomasz M / Kruszewski, Marcin

Molecular and cellular biochemistry

2014 Volume 389, Issue 1-2, Page(s) 99–111

Abstract: Pirin, a product of the PIR gene, is an iron-binding protein acting as a transcriptional coregulator implicated in the regulation of the NF-κB-related transcription via interaction with RelA (p65), as well as BCL3 and NF-κB1 (p50) proteins. Alterations ... ...

Abstract	Pirin, a product of the PIR gene, is an iron-binding protein acting as a transcriptional coregulator implicated in the regulation of the NF-κB-related transcription via interaction with RelA (p65), as well as BCL3 and NF-κB1 (p50) proteins. Alterations in pirin expression were observed in various tumors and under oxidative stress conditions. The aim of the present work was to analyze the regulation of the transcription of the human PIR gene. Using constructs containing a different sized PIR promoter and the luciferase reporter genes we found that in HeLa cells PIR transcription is mostly dependent on a highly conserved antioxidant response element located 281 bp downstream of the transcription start site. We have proved that the NRF2 transcription factor binds to this element in vivo and drives the basal PIR expression. We hypothesize that regulation of the PIR expression may constitute a mechanism by which NRF2 is able to modulate the activity of NF-κB and possibly other signaling pathways.
MeSH term(s)	Amino Acid Sequence ; Antioxidant Response Elements/genetics ; Carrier Proteins/genetics ; Cell Line, Tumor ; Dioxygenases ; Gene Expression Regulation/genetics ; HeLa Cells ; Humans ; Molecular Sequence Data ; NF-E2-Related Factor 2/genetics ; NF-kappa B/genetics ; Nuclear Proteins/genetics ; Promoter Regions, Genetic/genetics ; Sequence Alignment ; Signal Transduction/genetics ; Transcription Factors/genetics ; Transcription Initiation Site ; Transcription, Genetic/genetics
Chemical Substances	Carrier Proteins ; NF-E2-Related Factor 2 ; NF-kappa B ; NFE2L2 protein, human ; Nuclear Proteins ; Transcription Factors ; Dioxygenases (EC 1.13.11.-) ; PIR protein, human (EC 1.13.11.-)
Language	English
Publishing date	2014-01-05
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	184833-1
ISSN	1573-4919 ; 0300-8177
ISSN (online)	1573-4919
ISSN	0300-8177
DOI	10.1007/s11010-013-1931-0
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Zs.A 892: Show issues

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Article ; Online: Adaptation of HepG2 cells to silver nanoparticles-induced stress is based on the pro-proliferative and anti-apoptotic changes in gene expression.

Brzóska, Kamil / Męczyńska-Wielgosz, Sylwia / Stępkowski, Tomasz M / Kruszewski, Marcin

Mutagenesis

2015 Volume 30, Issue 3, Page(s) 431–439

Abstract: Silver nanoparticles (AgNPs) are one of the most widely used nanomaterials due to their antibacterial properties. Owing to the recent boost in the usage of AgNPs-containing products, human exposure to AgNPs is increasing, highlighting the need for ... ...

Abstract	Silver nanoparticles (AgNPs) are one of the most widely used nanomaterials due to their antibacterial properties. Owing to the recent boost in the usage of AgNPs-containing products, human exposure to AgNPs is increasing, highlighting the need for careful evaluation of AgNPs toxicity in humans. We used two cellular models, hepatic HepG2 and epithelial A549 cell lines, to study the mechanism of AgNPs-induced toxicity at the cellular level. These two cell lines differ significantly in their response to AgNPs treatment. In the case of A549 cells, a minor decrease in viability and increase in the extent of DNA breakage were observed. A markedly different response to AgNPs was observed in HepG2 cells. In short term, a massive induction of DNA breakage was observed, suggesting that the basal activity of antioxidant defence in these cells was not sufficient to effectively protect them from the nanoparticle-induced oxidative stress. After prolonged exposure, the extent of DNA breakage decreased to the level observed in the control cells proving that a successful adaptation to the new conditions had taken place. The cells that were unable to adapt must have died, as revealed by the Neutral Red assay that indicated less than half viable cells after 24-h treatment with 100 µg/ml of 20nm AgNPs. The gene expression analysis revealed that the observed adaptation was underlain by a pro-proliferative, anti-apoptotic signal leading to up-regulation of the genes promoting proliferation and inflammatory response (EGR1, FOS, JUN, HK2, IL4, MMP10, VEGFA, WISP1, CEBPB, IL8, SELPLG), genes coding the anti-apoptotic proteins (BCL2A1, CCL2) and factors involved in the response to stress (HSPB1, GADD45A). Such a selection of highly resistant population of cells should be taken into account in the case of medical applications of nanoparticles since the sustained proliferative signalling and resistance to cell death are hallmarks of cancer, acquired by the cells in the process of carcinogenesis.
MeSH term(s)	Adaptation, Physiological ; Apoptosis/drug effects ; Cell Proliferation/drug effects ; Cell Survival/drug effects ; DNA Damage ; Gene Expression/drug effects ; Hep G2 Cells ; Humans ; Metal Nanoparticles/toxicity ; Silver/toxicity
Chemical Substances	Silver (3M4G523W1G)
Language	English
Publishing date	2015-05
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	632903-2
ISSN	1464-3804 ; 0267-8357
ISSN (online)	1464-3804
ISSN	0267-8357
DOI	10.1093/mutage/gev001
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Zs.A 2189: Show issues

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Article ; Online: Putative proto-oncogene Pir expression is significantly up-regulated in the spleen and kidney of cytosolic superoxide dismutase-deficient mice.

Brzóska, Kamil / Stępkowski, Tomasz M / Kruszewski, Marcin

Redox report : communications in free radical research

2012 Volume 16, Issue 3, Page(s) 129–133

Abstract: Iron binding protein pirin was isolated as an interactor of the NFIX transcription factor but it can also form complexes with Bcl3 and NF-κB1(p50). Alterations of pirin expression were observed in various tumors and after exposure to pro-carcinogenic ... ...

Abstract	Iron binding protein pirin was isolated as an interactor of the NFIX transcription factor but it can also form complexes with Bcl3 and NF-κB1(p50). Alterations of pirin expression were observed in various tumors and after exposure to pro-carcinogenic oxidative stressors. The aim of the present work was to study the level of pirin transcription in an in vivo model of oxidative stress, namely, in Sod1-deficient mice. We have found that Sod1(-/-) mice have a significantly elevated level of Pir mRNA in the spleen and kidney but not in the liver, heart, or/and brain. We have also shown that similarly to its human ortholog, the mouse Pir gene transcription level varies significantly between organs. The highest expression was found in the liver and the lowest in the spleen and kidney. Based on literature data, we propose the involvement of Nrf2, AP-1, and NF-κB transcription factors in Pir up-regulation in Sod1(-/-) mice.
MeSH term(s)	Animals ; Carrier Proteins/metabolism ; Dioxygenases ; Female ; Gene Expression Regulation ; Genotype ; Kidney/metabolism ; Liver/metabolism ; Male ; Mice ; Mice, 129 Strain ; Mice, Knockout ; Models, Animal ; NF-kappa B p50 Subunit/genetics ; NF-kappa B p50 Subunit/metabolism ; NFI Transcription Factors/genetics ; NFI Transcription Factors/metabolism ; Nuclear Proteins/metabolism ; Oxidative Stress ; Promoter Regions, Genetic ; RNA, Messenger/metabolism ; Spleen/metabolism ; Superoxide Dismutase/deficiency ; Superoxide Dismutase/genetics ; Superoxide Dismutase/metabolism ; Transcription Factor AP-1/genetics ; Transcription Factor AP-1/metabolism ; Transcription, Genetic ; Up-Regulation
Chemical Substances	Carrier Proteins ; NF-kappa B p50 Subunit ; NFI Transcription Factors ; Nfix protein, mouse ; Nuclear Proteins ; RNA, Messenger ; Transcription Factor AP-1 ; Dioxygenases (EC 1.13.11.-) ; Pir protein, mouse (EC 1.13.11.-) ; Superoxide Dismutase (EC 1.15.1.1)
Language	English
Publishing date	2012-05-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1305290-1
ISSN	1743-2928 ; 1351-0002
ISSN (online)	1743-2928
ISSN	1351-0002
DOI	10.1179/1351000211Y.0000000002
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Article ; Online: The role of natural polyphenols in cell signaling and cytoprotection against cancer development.

Lewandowska, Hanna / Kalinowska, Monika / Lewandowski, Włodzimierz / Stępkowski, Tomasz M / Brzóska, Kamil

The Journal of nutritional biochemistry

2016 Volume 32, Page(s) 1–19

Abstract: The cytoprotective and anticancer action of dietary in-taken natural polyphenols has for long been attributed only to their direct radical scavenging activities. Currently it is well supported that those compounds display a broad spectrum of biological ... ...

Abstract	The cytoprotective and anticancer action of dietary in-taken natural polyphenols has for long been attributed only to their direct radical scavenging activities. Currently it is well supported that those compounds display a broad spectrum of biological and pharmacological outcomes mediated by their complex metabolism, interaction with gut microbiota as well as direct interactions of their metabolites with key cellular signaling proteins. The beneficial effects of natural polyphenols and their synthetic derivatives are extensively studied in context of cancer prophylaxis and therapy. Herein we focus on cell signaling to explain the beneficial role of polyphenols at the three stages of cancer development: we review the recent proceedings about the impact of polyphenols on the cytoprotective antioxidant response and their proapoptotic action at the premalignant stage, and finally we present data showing how phenolic acids (e.g., caffeic, chlorogenic acids) and flavonols (e.g., quercetin) hamper the development of metastatic cancer.
MeSH term(s)	Angiogenesis Inhibitors/metabolism ; Angiogenesis Inhibitors/therapeutic use ; Animals ; Anticarcinogenic Agents/metabolism ; Anticarcinogenic Agents/therapeutic use ; Apoptosis ; Autophagy ; Carcinogenesis ; Cinnamates/metabolism ; Cinnamates/therapeutic use ; Epigenesis, Genetic ; Flavonoids/metabolism ; Flavonoids/therapeutic use ; Free Radical Scavengers/metabolism ; Free Radical Scavengers/therapeutic use ; Healthy Diet ; Humans ; Models, Biological ; Neoplasm Metastasis/pathology ; Neoplasm Metastasis/prevention & control ; Neoplasm Metastasis/therapy ; Neoplasms/diet therapy ; Neoplasms/metabolism ; Neoplasms/pathology ; Neoplasms/prevention & control ; Neovascularization, Pathologic/diet therapy ; Neovascularization, Pathologic/metabolism ; Neovascularization, Pathologic/pathology ; Neovascularization, Pathologic/prevention & control ; Polyphenols/metabolism ; Polyphenols/therapeutic use ; Precancerous Conditions/diet therapy ; Precancerous Conditions/metabolism ; Precancerous Conditions/pathology ; Precancerous Conditions/prevention & control ; Signal Transduction
Chemical Substances	Angiogenesis Inhibitors ; Anticarcinogenic Agents ; Cinnamates ; Flavonoids ; Free Radical Scavengers ; Polyphenols
Language	English
Publishing date	2016
Publishing country	United States
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	1014929-6
ISSN	1873-4847 ; 0955-2863
ISSN (online)	1873-4847
ISSN	0955-2863
DOI	10.1016/j.jnutbio.2015.11.006
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Zs.A 2838: Show issues

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Article ; Online: LDL dinitrosyl iron complex acts as an iron donor in mouse macrophages.

Lewandowska, Hanna / Stępkowski, Tomasz M / Męczyńska-Wielgosz, Sylwia / Sikorska, Katarzyna / Sadło, Jarosław / Dudek, Jakub / Kruszewski, Marcin

Journal of inorganic biochemistry

2018 Volume 188, Page(s) 29–37

Abstract: Fe(NO) ...

Abstract	[Fe(NO)
MeSH term(s)	Animals ; Apolipoprotein B-100/chemistry ; Apolipoprotein B-100/pharmacology ; Iron/chemistry ; Iron/pharmacology ; Lipoproteins, LDL/chemistry ; Lipoproteins, LDL/pharmacology ; Macrophages/cytology ; Macrophages/metabolism ; Mice ; Nitrogen Oxides/chemistry ; Nitrogen Oxides/pharmacology ; RAW 264.7 Cells
Chemical Substances	Apolipoprotein B-100 ; Lipoproteins, LDL ; Nitrogen Oxides ; dinitrosyl iron complex (68586-27-6) ; Iron (E1UOL152H7)
Language	English
Publishing date	2018-08-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	162843-4
ISSN	1873-3344 ; 0162-0134
ISSN (online)	1873-3344
ISSN	0162-0134
DOI	10.1016/j.jinorgbio.2018.08.004
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Article: Molecular cross-talk between the NRF2/KEAP1 signaling pathway, autophagy, and apoptosis

Stępkowski, Tomasz M / Kruszewski, Marcin K

Free Radical Biology and Medicine. 2011 May 1, v. 50, no. 9

2011

Abstract	Oxidative stress, perturbations in the cellular thiol level and redox balance, affects many cellular functions, including signaling pathways. This, in turn, may cause the induction of autophagy or apoptosis. The NRF2/KEAP1 signaling pathway is the main pathway responsible for cell defense against oxidative stress and maintaining the cellular redox balance at physiological levels. The relation between NRF2/KEAP1 signaling and regulation of apoptosis and autophagy is not well understood. In this hypothesis article we discuss how KEAP1 protein and its direct interactants (such as PGAM5, prothymosin α, FAC1 (BPTF), and p62) provide a molecular foundation for a possible cross-talk between NRF2/KEAP1, apoptosis, and autophagy pathways. We present a hypothesis for how NRF2/KEAP1 may interfere with the cellular apoptosis-regulatory machinery through activation of the ASK1 kinase by a KEAP1 binding partner—PGAM5. Based on very recent experimental evidence, new hypotheses for a cross-talk between NF-κB and the NRF2/KEAP1 pathway in the context of autophagy-related “molecular hub” protein p62 are also presented. The roles of KEAP1 molecular binding partners in apoptosis regulation during carcinogenesis and in neurodegenerative diseases are also discussed.
Keywords	apoptosis ; autophagy ; carcinogenesis ; neurodegenerative diseases ; oxidative stress ; signal transduction ; thiols ; transcription factor NF-kappa B
Language	English
Dates of publication	2011-0501
Size	p. 1186-1195.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	807032-5
ISSN	1873-4596 ; 0891-5849
ISSN (online)	1873-4596
ISSN	0891-5849
DOI	10.1016/j.freeradbiomed.2011.01.033
Database	NAL-Catalogue (AGRICOLA)

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Zs.A 2109: Show issues

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