ArticleBiochemistry2016
Curcumin Inhibits Protein Kinase Cα Activity by Binding to Its C1 Domain.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Protein Kinase C Family: Structures, Biological Functions, Diseases, and Pharmaceutical Interventions.MedComm · 2025Review
- Plant food-derived antioxidant nutrients in neuroprotection against chemotherapy-induced neurotoxicity: from molecular mechanisms to clinical applications.Frontiers in nutrition · 2025Review
- Investigation of the Effect of Curcumin on Protein Targets in NAFLD Using Bioinformatic Analysis.Nutrients · 2022Article
- Putative role of natural products as Protein Kinase C modulator in different disease conditions.Daru : journal of Faculty of Pharmacy, Tehran University of Medical Sciences · 2021Review
- Probing the Diacylglycerol Binding Site of Presynaptic Munc13-1.Biochemistry · 2021Article
- Anti-Malignant Ascites Effect of Total Diterpenoids fromMolecules (Basel, Switzerland) · 2021Article
- Compounds from Natural Sources as Protein Kinase Inhibitors.Biomolecules · 2020Review
- Munc13 Is a Molecular Target of Bryostatin 1.Biochemistry · 2019Article
- Resveratrol inhibits phorbol ester-induced membrane translocation of presynaptic Munc13-1.Biochimica et biophysica acta. General subjects · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Curcumin is a polyphenolic nutraceutical that acts on multiple biological targets, including protein kinase C (PKC). PKC is a family of serine/threonine kinases central to intracellular signal transduction. We have recently shown that curcumin selectively inhibits PKCα, but not PKCε, in CHO-K1 cells [Pany, S. (2016) Biochemistry 55, 2135-2143]. To understand which domain(s) of PKCα is responsible for curcumin binding and inhibitory activity, we made several domain-swapped mutants in which the C1 (combination of C1A and C1B) and C2 domains are swapped between PKCα and PKCε. Phorbol ester-induced membrane translocation studies using confocal microscopy and immunoblotting revealed that curcumin inhibited phorbol ester-induced membrane translocation of PKCε mutants, in which the εC1 domain was replaced with αC1, but not the PKCα mutant in which αC1 was replaced with the εC1 domain, suggesting that αC1 is a determinant for curcumin's inhibitory effect. In addition, curcumin inhibited membrane translocation of PKCε mutants, in which the εC1A and εC1B domains were replaced with the αC1A and αC1B domains, respectively, indicating the role of both αC1A and αC1B domains in curcumin's inhibitory effects. Phorbol 13-acetate inhibited the binding of curcumin to αC1A and αC1B with IC
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