ArticleThe Biochemical journal2000
Protein kinase C activation by acidic proteins including 14-3-3.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 48 citations in OpenAlex.
- Human TNF-α induces differential protein phosphorylation in Schistosoma mansoni adult male worms.Parasitology research · 2016Article
- Early down-regulation of PKCδ as a pro-survival mechanism in Huntington's disease.Neuromolecular medicine · 2014Article
- 14-3-3 Proteins are Regulators of Autophagy.Cells · 2012Article
- 14-3-3ζ interacts with stat3 and regulates its constitutive activation in multiple myeloma cells.PloS one · 2012Article
- Cancer secretomics reveal pathophysiological pathways in cancer molecular oncology.Molecular oncology · 2010Review
- Overexpression of xCT induces up-regulation of 14-3-3beta in Kaposi's sarcoma.Bioscience reports · 2010Article
- Tandem phosphorylation of serines 221 and 318 by protein kinase Cdelta coordinates mRNA binding and nucleocytoplasmic shuttling of HuR.Molecular and cellular biology · 2010Article
- Differential activation of extracellular signal-regulated kinase 1 and a related complex in neuronal nuclei.Brain cell biology · 2006Article
- Integration of P2Y receptor-activated signal transduction pathways in G protein-dependent signalling networks.Purinergic signalling · 2006Article
- Article
- Expression of 14-3-3 zeta and interaction with protein kinase C in the rat retina in early diabetes.Diabetologia · 2005Article
- Adaptative value of a PKC-PKI55 feedback loop of inhibition that prevents the kinase's deregulation.Journal of molecular evolution · 2003Article
- Tenascin-C signaling through induction of 14-3-3 tau.The Journal of cell biology · 2003Article
- Functional specificity in 14-3-3 isoform interactions through dimer formation and phosphorylation. Chromosome location of mammalian isoforms and variants.Plant molecular biology · 2002Review
- A role for alpha-synuclein in the regulation of dopamine biosynthesis.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
14-3-3 proteins may function as adapter or scaffold proteins in signal transduction pathways. We reported previously that several 14-3-3 isotypes bind to protein kinase C (PKC)-zeta and facilitate coupling of PKC-zeta to Raf-1 [van der Hoeven, van der Wal, Ruurs, van Dijk and van Blitterswijk (2000) Biochem. J. 345, 297-306], an event that boosts the mitogen-activated protein kinase (ERK) pathway in Rat-1 fibroblasts. The present work investigated whether bound 14-3-3 would affect PKC-zeta activity. Using recombinant 14-3-3 proteins and purified PKC-zeta in a convenient, newly developed in vitro kinase assay, we found that 14-3-3 proteins stimulated PKC-zeta activity in a dose-dependent fashion up to approx. 2.5-fold. Activation of PKC-zeta by 14-3-3 isotypes was unrelated to their mutual affinity, estimated by co-immunoprecipitation from COS cell lysates. Accordingly, PKC-zeta with a defective (point-mutated) 14-3-3-binding site, showed the same 14-3-3-stimulated activity as wild-type PKC-zeta. As 14-13-3 proteins are acidic, we tested several other acidic proteins, which turned out to stimulate PKC-zeta activity in a similar fashion, whereas neutral or basic proteins did not. These effects were not restricted to the atypical PKC-zeta, but were also found for classical PKC. Together, the results suggest that the stimulation of PKC activity by 14-3-3 proteins is non-specific and solely due to the acidic nature of these proteins, quite similar to that known for acidic lipids.
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