14‐3‐3 proteins bind to histone and affect both histone phosphorylation and dephosphorylation
- 27 June 1994
- journal article
- Published by Wiley in FEBS Letters
- Vol. 347 (2-3) , 128-132
- https://doi.org/10.1016/0014-5793(94)00520-6
Abstract
14‐3‐3 proteins appear to play a critical role in Ca2+‐stimulated secretion in permeabilized chromaffin cells. 14‐3‐3 proteins have been reported to be both stimulators and inhibitors of protein kinase C (PKC). We have found that 14‐3‐3 proteins, isolated on the basis of their ability to enhance secretory activity, stimulated histone phosphorylation by PKC, but they had no effect on myosin light chain phosphorylation by PKC. 14‐3‐3 proteins were also found to inhibit the rate of [32P]histone dephosphorylation but not the rate of [32P]myosin light chain dephosphorylation. Cross‐linking experiments and affinity chromatography demonstrated that 14‐3‐3 proteins bind to histones. These results suggest that at least some of the reported effects of 14‐3‐3 proteins on PKC activity may result from 14‐3‐3 proteins binding to histone.Keywords
This publication has 32 references indexed in Scilit:
- Brain 14‐3‐3 protein is an activator protein that activates tryptophan 5‐monooxygenase and tyrosine 3‐monooxygenase in the presence of Ca2+,calmodulin‐dependent protein kinase IIPublished by Wiley ,2001
- Activation of protein kinase C by the 14‐3‐3 proteins homologous with Exol protein that stimulates calcium‐dependent exocytosisFEBS Letters, 1992
- Exol and Exo2 proteins stimulate calcium-dependent exocytosis in permeabilized adrenal chromaff in cellsNature, 1992
- Calpactin‐depleted cytosolic proteins restore Ca2+‐dependent secretion to digitonin‐permeabilized bovine chromaffin cellsFEBS Letters, 1991
- Widespread Distribution of the 14-3-3 Protein in Vertebrate Brains and Bovine Tissues: Correlation with the Distributions of Calcium-Dependent Protein KinasesJournal of Neurochemistry, 1991
- Distinct forms of the protein kinase-dependent activator of tyrosine and tryptophan hydroxylasesJournal of Molecular Biology, 1991
- Protein kinase C inhibitor proteinsEuropean Journal of Biochemistry, 1990
- Calyculin A and okadaic acid: Inhibitors of protein phosphatase activityBiochemical and Biophysical Research Communications, 1989
- Stimulation by inositol trisphosphate and tetrakisphosphate of a protein phosphataseBiochemical and Biophysical Research Communications, 1988
- The Protein Phosphatases Invloved in Cellular Regulation. 4. Classification of Two Homogeneous Myosin Light Chain Phosphatases from Smoth Muscle as Protein Phosphatase-2A1 and 2C, and a Homogeneous Protein Phosphatase from Reticulocytes Active on Protein Synthesis Initiation Factor eIF-2 as Protein Phosphatase-2A2European Journal of Biochemistry, 1983