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• W1948946196 endingPage "11710" @default.
• W1948946196 startingPage "11698" @default.
• W1948946196 abstract "We studied the effects of phosphorylation by protein kinase A (PKA) on GABA(A) receptors (alpha1beta1gamma2L andalpha1beta3gamma2L) transiently expressed in HEK 293T cells. Under conditions favorable for PKA activation, currents obtained using whole-cell patch clamp of lifted cells displayed increased rate and extent of the fast phases of desensitization, decreased rate of current deactivation after GABA removal, and prolongation of brief IPSC-like currents. Mutation of serine residues (beta1 S409, beta3 S407, beta3 S408) revealed that only beta1 S409 and beta3 S408 were critical for the modulatory effect of PKA on GABA(A) receptor currents. Additionally, repeated pulse inhibition was increased in receptors after mutation of the critical serine to glutamate and decreased when the serine was mutated to alanine. These data demonstrate that PKA phosphorylation modulated GABA(A) receptor currents by increasing fast phases of macroscopic desensitization and suggest a role for PKA in regulating GABAergic IPSC duration." @default.
• W1948946196 created "2016-06-24" @default.
• W1948946196 creator A5044198884 @default.
• W1948946196 creator A5068641472 @default.
• W1948946196 date "2003-12-17" @default.
• W1948946196 modified "2023-10-13" @default.
• W1948946196 title "β Subunit Phosphorylation Selectively Increases Fast Desensitization and Prolongs Deactivation of α1β1γ2L and α1β3γ2L GABA_AReceptor Currents" @default.
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• W1948946196 doi "https://doi.org/10.1523/jneurosci.23-37-11698.2003" @default.
• W1948946196 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6740942" @default.
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