Phosphorylation of the receptor for immunoglobulin E
- 27 April 1982
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 21 (9) , 2004-2010
- https://doi.org/10.1021/bi00538a005
Abstract
Specific immune precipitation of IgE-receptor complexes from detergent extracts of 32P-labeled rat basophilic leukemia cells yielded a phosphoprotein of MW 35,000 on gel electrophoresis in sodium dodecyl sulfate. This phosphoprotein was shown by several criteria to be the .beta. chain of the receptor for IgE. Phosphorylation occurs at a serine residue (or residues) in a region (.beta.2) of the .beta. chain that is thought to be exposed on the cytoplasmic face of the plasma membrane. Phosphorylation probably takes place after the insertion of the .beta. chain into the membrane. The IgE-binding .alpha. chain of the receptor and the IgE associated with it are not phosphorylated. No changes have been determined so far in the state of phosphorylation of either chain of the receptor or of IgE itself after IgE-mediated triggering of the cells.This publication has 1 reference indexed in Scilit:
- Stimulation of phospholipid methylation, Ca2+ influx, and histamine release by bridging of IgE receptors on rat mast cells.Proceedings of the National Academy of Sciences, 1980