ArticleAntioxidants & redox signaling2011
Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation?
Article in Antioxidants & redox signaling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
11 citing papers in PubMed, 29 citations in OpenAlex.
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- Quantum chemistry rules retinoid biology.Communications biology · 2023Review
- Munc13 structural transitions and oligomers that may choreograph successive stages in vesicle priming for neurotransmitter release.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The mitochondrial PKCδ/retinol signal complex exerts real-time control on energy homeostasis.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
- TrypOx, a Novel Eukaryotic Homolog of the Redox-Regulated Chaperone Hsp33 inFrontiers in microbiology · 2020Article
- Retinol as a cofactor for PKCδ-mediated impairment of insulin sensitivity in a mouse model of diet-induced obesity.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2016Article
- Retinol as electron carrier in redox signaling, a new frontier in vitamin A research.Hepatobiliary surgery and nutrition · 2016Review
- Thiol-based redox switches.Biochimica et biophysica acta · 2014Review
- Protein redox chemistry: post-translational cysteine modifications that regulate signal transduction and drug pharmacology.Frontiers in pharmacology · 2014Article
- Nitric oxide and zinc-mediated protein assemblies involved in mu opioid receptor signaling.Molecular neurobiology · 2013Review
- Two protein kinase C isoforms, δ and ε, regulate energy homeostasis in mitochondria by transmitting opposing signals to the pyruvate dehydrogenase complex.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
Corrections and comments
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Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
Protein kinase C (PKC) is activated by lipid second messengers or redox action, raising the question whether these activation modes involve the same or alternate mechanisms. Here we show that both lipid activators and oxidation target the zinc-finger domains of PKC, suggesting a unifying activation mechanism. We found that lipid agonist-binding or redox action leads to zinc release and disassembly of zinc fingers, thus triggering large-scale unfolding that underlies conversion to the active enzyme. These results suggest that PKC zinc fingers, originally considered purely structural devices, are in fact redox-sensitive flexible hinges, whose conformation is controlled both by redox conditions and lipid agonists.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.