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We studied the effects of phosphorylation by protein kinase A (PKA) on GABAA receptors (α1β1γ2L andα1β3γ2L) 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 (β1 S409, β3 S407, β3 S408) revealed that only β1 S409 and β3 S408 were critical for the modulatory effect of PKA on GABAA 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 GABAA receptor currents by increasing fast phases of macroscopic desensitization and suggest a role for PKA in regulating GABAergic IPSC duration.

the journal of neuroscience/the journal of neuroscience

β Subunit Phosphorylation Selectively Increases Fast Desensitization and Prolongs Deactivation of α1β1γ2L and α1β3γ2L GABA<sub>A</sub>Receptor Currents

β Subunit Phosphorylation Selectively Increases Fast Desensitization and Prolongs Deactivation of α1β1γ2L and α1β3γ2L GABAAReceptor Currents

β Subunit Phosphorylation Selectively Increases Fast Desensitization and Prolongs Deactivation of α1β1γ2L and α1β3γ2L GABA_AReceptor Currents