We have found that the acetylcholine receptor (AChR) of Torpedo californica is phosphorylated and dephosphorylated in situ by a membrane-bound protein kinase and phosphatase [1]. There is increasing evidence that other neurotransmitters [2], light [3-6], polypeptide hormones [7], and growth factors
Phosphorylation of the membrane-bound acetylcholine receptor: Inhibition by diphenylhydantoin
β Scribed by Adrienne S. Gordon; Dale Milfay; Dr Ivan Diamond
- Publisher
- John Wiley and Sons
- Year
- 1979
- Tongue
- English
- Weight
- 290 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0364-5134
No coin nor oath required. For personal study only.
β¦ Synopsis
Abstract
Purified postsynaptic membranes can be used as a model system to study the regulation of synaptic membrane proteins. These membranes contain protein kinase activity that phosphorylates the acetylcholine receptor (AChR). We find that diphenylhydantoin (DPH) interacts with these membranes to inhibit phosphorylation of the membraneβbound AChR. DPH appears to alter the availability of postsynaptic membrane proteins for phosphorylation by a synaptic membrane protein kinase. The concentration of DPH that produces halfβmaximal inhibition of AChR phosphorylation is about 5 Γ 10^β5^ M. This suggests that one of the specific effects of DPH in the nervous system may be related to inhibition of phosphorylation of postsynaptic membrane proteins.
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