Phosphorylation of membrane-bound acetylcholine receptor by protein kinase C: characterization and subunit specificity
- 17 July 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (28) , 6730-6734
- https://doi.org/10.1021/bi00480a024
Abstract
Acetylcholine receptor (AChR) from Torpedo electric organ in its membrane-bound or solubilized form is phosphorylated by the Ca2+/phospholipid-dependent protein kinase (PKC). The subunit specificity for PKC is different from that observed for cAMP-dependent protein kinase (PKA). Whereas PKC phosphorylates predominantly the .delta. subunit and the phosphorylation of the .gamma. subunit by this enzyme is very low, PKA phosphorylates both subunits to a similar high extent. We have extended our phosphorylation studies to a synthetic peptide from the .gamma. subunit, corresponding to residues 346-359, which contains a consensus PKA phosphorylation site. This synthetic peptide is phosphorylated by both PKA and PKC, suggesting that in the intact receptor both kinases may phosphorylate the .gamma. subunit at a similar site, as has been previously demonstrated by us for the .delta. subunit [Safran A., et. al. (1987) J. Biol. Chem. 262, 10506-10510]. The diverse pattern of phosphorylation of AChR by PKA and PKC may play a role in the regulation of its function.This publication has 22 references indexed in Scilit:
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