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NMDA receptor-dependent GABA(B) receptor internalization via CaMKII phosphorylation of serine 867 in GABA(B1)
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SYSNO ASEP 0347602 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title NMDA receptor-dependent GABA(B) receptor internalization via CaMKII phosphorylation of serine 867 in GABA(B1) Author(s) Guetg, N. (CH)
Aziz, S. A. (CH)
Holbro, N. (CH)
Tureček, Rostislav (UEM-P) RID, ORCID
Rose, T. (CH)
Seddik, R. (CH)
Gassmann, M. (CH)
Moes, S. (CH)
Jenoe, P. (CH)
Oertner, T.G. (CH)
Casanova, E. (CH)
Bettler, B. (CH)Source Title Proceedings of the National Academy of Sciences of the United States of America. - : National Academy of Sciences - ISSN 0027-8424
Roč. 107, č. 31 (2010), s. 13924-13929Number of pages 6 s. Language eng - English Country US - United States Keywords gamma-aminobutyric acid ; spines ; trafficking Subject RIV FH - Neurology CEZ AV0Z50390512 - UEM-P (2005-2011) UT WOS 000280605900067 DOI 10.1073/pnas.1000909107 Annotation We have found that NMDA receptor activation promotes dynamin-dependent endocytosis of GABA(B) receptors by Ca2+/Calmodulin-dependent protein kinase II (CaMKII) mechanism. CaMKII associates with GABA(B) in vivo and phosphorylates serine 867 (S867) in the intracellular C terminus of the GABA(B1) subunit. Time-lapse two-photon imaging of organotypic hippocampal slices reveals that activation of NMDA receptors removes GABA(B) receptors within minutes from the surface of dendritic spines and shafts. NMDA-dependent GABA(B) internalization is represents a novel form of synaptic plasticity Workplace Institute of Experimental Medicine Contact Lenka Koželská, lenka.kozelska@iem.cas.cz, Tel.: 241 062 218, 296 442 218 Year of Publishing 2011
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