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• W2103208153 abstract "GABA A receptors are critical in controlling neuronal activity. Here, we examined the role for phospholipase C-related inactive protein type 1 (PRIP-1), which binds and inactivates protein phosphatase 1α (PP1α) in facilitating GABA A receptor phospho-dependent regulation using PRIP-1 -/- mice. In wild-type animals, robust phosphorylation and functional modulation of GABA A receptors containing β3 subunits by cAMP-dependent protein kinase was evident, which was diminished in PRIP-1 -/- mice. PRIP-1 -/- mice exhibited enhanced PP1α activity compared with controls. Furthermore, PRIP-1 was able to interact directly with GABA A receptor β subunits, and moreover, these proteins were found to be PP1α substrates. Finally, phosphorylation of PRIP-1 on threonine 94 facilitated the dissociation of PP1α-PRIP-1 complexes, providing a local mechanism for the activation of PP1α. Together, these results suggest an essential role for PRIP-1 in controlling GABA A receptor activity via regulating subunit phosphorylation and thereby the efficacy of neuronal inhibition mediated by these receptors." @default.
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• W2103208153 date "2004-08-11" @default.
• W2103208153 modified "2023-10-17" @default.
• W2103208153 title "GABA_AReceptor Phospho-Dependent Modulation Is Regulated by Phospholipase C-Related Inactive Protein Type 1, a Novel Protein Phosphatase 1 Anchoring Protein" @default.
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• W2103208153 doi "https://doi.org/10.1523/jneurosci.1323-04.2004" @default.
• W2103208153 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6729171" @default.
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