Phosphorylation on Ser-359 of the α2 subunit in GABA type A receptors down-regulates their density at inhibitory synapses.

ABSTRACT: GABA type A receptors (GABA_ARs) mediate fast synaptic inhibition and are trafficked to functionally diverse synapses. However, the precise molecular mechanisms that regulate the synaptic targeting of these receptors are unclear. Whereas it has been previously shown that phosphorylation events in α4, β, and γ subunits of GABA_ARs govern their function and trafficking, phosphorylation of other subunits has not yet been demonstrated. Here, we show that the α2 subunit of GABA_ARs is phosphorylated at Ser-359 and enables dynamic regulation of GABA_AR binding to the scaffolding proteins gephyrin and collybistin. We initially identified Ser-359 phosphorylation by MS analysis, and additional experiments revealed that it is regulated by the activities of cAM

SUBMITTER: Nakamura Y 

PROVIDER: S-EPMC7458806 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature