Number of the records: 1  

NMDA receptor-dependent GABA(B) receptor internalization via CaMKII phosphorylation of serine 867 in GABA(B1)

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    SYSNO ASEP0347602
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleNMDA 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 TitleProceedings 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. 13924-13929
    Number of pages6 s.
    Languageeng - English
    CountryUS - United States
    Keywordsgamma-aminobutyric acid ; spines ; trafficking
    Subject RIVFH - Neurology
    CEZAV0Z50390512 - UEM-P (2005-2011)
    UT WOS000280605900067
    DOI10.1073/pnas.1000909107
    AnnotationWe 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
    WorkplaceInstitute of Experimental Medicine
    ContactLenka Koželská, lenka.kozelska@iem.cas.cz, Tel.: 241 062 218, 296 442 218
    Year of Publishing2011
Number of the records: 1  

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