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The Journal of Neuroscience, August 11, 2004, 24(32):7074-7084; doi:10.1523/JNEUROSCI.1323-04.2004

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Cellular/Molecular
GABA_A Receptor Phospho-Dependent Modulation Is Regulated by Phospholipase C-Related Inactive Protein Type 1, a Novel Protein Phosphatase 1 Anchoring Protein

Miho Terunuma,¹ Il-Sung Jang,² Sang Hoon Ha,⁵ Josef T. Kittler,⁴ Takashi Kanematsu,¹ Jasmina N. Jovanovic,⁴ Keiichi I. Nakayama,³ Norio Akaike,² Sung Ho Ryu,⁵ Stephen J. Moss,⁶ and Masato Hirata¹

¹Laboratory of Molecular and Cellular Biochemistry, Faculty of Dental Science and Station for Collaborative Research, ²Laboratory of Cellular and System Physiology, Faculty of Medical Science, and ³Department of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan, ⁴Medical Research Council Laboratory of Molecular Cell Biology and Department of Pharmacology, University College London, London WC1E 6BT, United Kingdom, ⁵Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, South Korea, and ⁶Department of Neuroscience, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-6058

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 1 (PP1) 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 3 subunits by cAMP-dependent protein kinase was evident, which was diminished in PRIP-1^-/- mice. PRIP-1^-/- mice exhibited enhanced PP1 activity compared with controls. Furthermore, PRIP-1 was able to interact directly with GABA_A receptor subunits, and moreover, these proteins were found to be PP1 substrates. Finally, phosphorylation of PRIP-1 on threonine 94 facilitated the dissociation of PP1-PRIP-1 complexes, providing a local mechanism for the activation of PP1. 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.

Key words: GABA; receptor; phosphorylation; phosphatase; protein kinase; cAMP

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Received April 8, 2004; revised May 25, 2004; accepted June 16, 2004.

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