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Neuronal activity regulates phosphorylation-dependent surface delivery of G protein-activated inwardly rectifying potassium channels.

Authors: Chung, HJ  Qian, X  Ehlers, M  Jan, YN  Jan, LY 
Citation: Chung HJ, etal., Proc Natl Acad Sci U S A. 2009 Jan 13;106(2):629-34. Epub 2008 Dec 31.
Pubmed: (View Article at PubMed) PMID:19118198
DOI: Full-text: DOI:10.1073/pnas.0811615106

G protein-activated inwardly rectifying K(+) (GIRK) channels regulate neuronal excitability by mediating inhibitory effects of G protein-coupled receptors for neurotransmitters and neuromodulators. Notwithstanding many studies reporting modulation of GIRK channel function, whether neuronal activity regulates GIRK channel trafficking remains an open question. Here we report that NMDA receptor activation in cultured dissociated hippocampal neurons elevates surface expression of the GIRK channel subunits GIRK1 and GIRK2 in the soma, dendrites, and dendritic spines within 15 min. This activity-induced increase in GIRK surface expression requires protein phosphatase-1-mediated dephosphorylation of a serine residue (Ser-9) preceding the GIRK2 Val-13/Leu-14 (VL) internalization motif, thereby promoting channel recycling. Because activation of GIRK channels hyperpolarizes neuronal membranes, the NMDA receptor-induced regulation of GIRK channel trafficking may represent a dynamic adjustment of neuronal excitability in response to inhibitory neurotransmitters and/or neuromodulators.

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CRRD Object Information
CRRD ID: 2316501
Created: 2010-02-12
Species: All species
Last Modified: 2010-02-12
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.