Phosphorylation of liver gap junction protein by protein kinase C
Open Access
- 5 January 1987
- journal article
- Published by Wiley in FEBS Letters
- Vol. 210 (2) , 169-172
- https://doi.org/10.1016/0014-5793(87)81330-3
Abstract
The 27 kDa protein, a major component of rat liver gap junctions, was shown to be phosphorylated in vitro by protein kinase C. The stoichiometry of the phosphorylation indicated that approx. 0.33 mol phosphate was incorporated per mol 27 kDa protein. Phosphorylation was entirely dependent on the presence of calcium and was virtually specific for serine residues. For comparison, the gap junction protein was also examined for its phosphorylation by cAMP‐dependent protein kinase, the extent of phosphorylation being one‐tenth that exerted by protein kinase C.Keywords
This publication has 18 references indexed in Scilit:
- Cloning and characterization of human and rat liver cDNAs coding for a gap junction protein.The Journal of cell biology, 1986
- Studies and Perspectives of Protein Kinase CScience, 1986
- Physiology and Pharmacology of Gap JunctionsAnnual Review of Physiology, 1985
- Diacylglycerol inhibits gap junctional communication in cultured epidermal cells: Evidence for a role of protein kinase CBiochemical and Biophysical Research Communications, 1985
- Differences between liver gap junction protein and lens MIP 26 from rat: Implications for tissue specificity of gap junctionsCell, 1983
- Structure of the junction between communicating cellsNature, 1980
- Tumor promoters inhibit metabolic cooperation in cocultures of epidermal and 3T3 cellsBiochemical and Biophysical Research Communications, 1979
- Structure and biochemistry of mouse hepatic gap junctionsJournal of Molecular Biology, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970