ArticleMolecular and cellular biochemistry
Post-translationally modified 14-3-3 isoforms and inhibition of protein kinase C.
Article in Molecular and cellular biochemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 69 citations in OpenAlex.
- 14-3-3 proteins: Regulators of cardiac excitation-contraction coupling and stress responses.The Journal of physiology · 2026Review
- Glycoprotein Ibα-Dependent Platelet Activation is Essential for Tumor Cell-Platelet Interaction and Experimental Metastasis.MedComm · 2025Article
- Essential role of glycoprotein Ibα in platelet activation.Blood advances · 2024Article
- Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response.Nature reviews. Molecular cell biology · 2013Review
- Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patterns.Cell cycle (Georgetown, Tex.) · 2008Article
- Microphthalmia-associated transcription factor interactions with 14-3-3 modulate differentiation of committed myeloid precursors.Molecular biology of the cell · 2006Article
- Expression of 14-3-3 zeta and interaction with protein kinase C in the rat retina in early diabetes.Diabetologia · 2005Article
- Activity-dependent expression of acyl-coenzyme a-binding protein in retinal muller glial cells evoked by optokinetic stimulation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004Article
- Proteomic identification of 14-3-3zeta as a mitogen-activated protein kinase-activated protein kinase 2 substrate: role in dimer formation and ligand binding.Molecular and cellular biology · 2003Article
- Consummating signal transduction: the role of 14-3-3 proteins in the completion of signal-induced transitions in protein activity.The Plant cell · 2002Review
- 14-3-3 proteins; bringing new definitions to scaffolding.Oncogene · 2001Review
- Regulation of the Raf-1 kinase domain by phosphorylation and 14-3-3 association.The Biochemical journal · 2000Article
- Protein kinase C activation by acidic proteins including 14-3-3.The Biochemical journal · 2000Article
- Maintenance of genomic integrity by p53: complementary roles for activated and non-activated p53.Oncogene · 1999Review
- alpha-Synuclein shares physical and functional homology with 14-3-3 proteins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
- The regulation of neurotransmitter secretion by protein kinase C.Molecular neurobiology · 1998Review
- 14-3-3 proteins in neuronal development and function.Molecular neurobiology · 1998Review
- 14-3-3 inhibits the Dictyostelium myosin II heavy-chain-specific protein kinase C activity by a direct interaction: identification of the 14-3-3 binding domain.Molecular biology of the cell · 1997Article
- Structure and sites of phosphorylation of 14-3-3 protein: role in coordinating signal transduction pathways.Journal of protein chemistry · 1997Article
- Identification of 14-3-3 proteins in human platelets: effects of synthetic peptides on protein kinase C activation.The Biochemical journal · 1996Article
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
Abstract
This report compares the ability of individual members of the 14-3-3 protein family to inhibit particular protein kinase C (PKC) isoforms. We also show that two of these 14-3-3 isoforms (alpha and delta) specific to mammalian and avian brain are in vivo post-translationally modified forms of beta and zeta respectively. The presence of this modification enhances the activity of 14-3-3 as an inhibitor of protein kinase C nearly two fold. A method for analysing isoforms of 14-3-3 on acid-urea gels is also described. This permits the complete separation of all major isoforms and their unequivocal identification by a range of isoform specific antisera. The activity of recombinant 14-3-3 and isoforms renatured by a novel method after separation by reverse phase HPLC are compared. The effects of diacylglycerol and the phorbol ester, PMA (phorbol 1 2-myristate 13 acetate) on the inhibition suggest that one of the sites of interaction of 14-3-3 may be the cysteine-rich (C1) domain in PKC.
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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.