Cited by 300Genomics, phytochemicals, and oxidative stressRedox biology and oxidative stressGlutathione Transferases and Polymorphisms

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PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria

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Lo, Shih-Ching, Hannink, Mark·2008·Experimental Cell Research

DOI 10.1016/j.yexcr.2008.02.014PMC PMC2409987

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Abstract

Eukaryote cells balance production of reactive oxygen species (ROS) with levels of anti-oxidant enzyme activity to maintain cellular redox homeostasis. Mitochondria are a major source of ROS, while many anti-oxidant genes are regulated by the Nrf2 transcription factor. Keap1, a redox-regulated substrate adaptor for a cullin-based ubiquitin ligase, targets Nrf2 for proteosome-mediated degradation and represses Nrf2-dependent gene expression. We have previously identified a member of the phosphoglycerate mutase family, PGAM5, as a Keap1-binding protein. In this report, we demonstrate that PGAM5 is targeted to the outer membrane of mitochondria by an N-terminal mitochondrial-localization sequence. Furthermore, we provide evidence that PGAM5 forms a ternary complex containing both Keap1 and Nrf2, in which the dimeric Keap1 protein simultaneously binds both PGAM5 and Nrf2 through their conserved E(S/T)GE motifs. Knockdown of either Keap1 or PGAM5 activates Nrf2-dependent gene expression. We suggest that this ternary complex provides a molecular framework for understanding how nuclear anti-oxidant gene expression is regulated in response to changes in mitochondrial function(s).

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Authors: Lo, S.-C., & Hannink, M.
Affiliations: University of Missouri (US)
Corresponding author: Hannink, Mark
ORCID: Lo, Shih-Ching
Hannink, Mark
Venue: Experimental Cell Research
Publisher: Elsevier BV
Published: 2008-05
Volume: 314
Issue: 8
Pages: 1789-1803
ISSN: 0014-4827 (ISSN-L)
DOI: 10.1016/j.yexcr.2008.02.014
PMC: PMC2409987
OpenAlex: W1974124666
Cited by: 300
References: 82
Citations by year: 2026: 10 · 2025: 13 · 2024: 19 · 2023: 22 · 2022: 22 · 2021: 29 · 2020: 29 · 2019: 15 · 2018: 18 · 2017: 17 · 2016: 19 · 2015: 17 · 2014: 16 · 2013: 14 · 2012: 17
FWCI: 2.88
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Experimental Cell Research (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institutes of Health (1 RO1 AT003389)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Keywords: PGAM5, Keap1, Nrf2, ternary complex, mitochondrial outer membrane, redox homeostasis, reactive oxygen species, antioxidant gene expression, proteasomal degradation
MeSH terms: Kelch-Like ECH-Associated Protein 1, Amino Acid Sequence, Animals, Carrier Proteins, Cell Line, Cell Nucleus, Gene Expression Regulation, Humans, Mitochondria, Molecular Sequence Data, Phosphoglycerate Mutase, Phosphoprotein Phosphatases, Protein Isoforms, Protein Sorting Signals, Mitochondrial Proteins, Intracellular Signaling Peptides and Proteins, NF-E2-Related Factor 2

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PGAM5 tethers a ternary complex containing Keap1 and Nrf2 to mitochondria

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