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Regulation of AMPA receptor trafficking by O-glycosylation.

Authors: Kanno, T  Yaguchi, T  Nagata, T  Mukasa, T  Nishizaki, T 
Citation: Kanno T, etal., Neurochem Res. 2010 May;35(5):782-8. Epub 2010 Feb 18.
Pubmed: (View Article at PubMed) PMID:20165912
DOI: Full-text: DOI:10.1007/s11064-010-0135-1

The present study investigated the role of O-linked beta-N-acetylglucosamine (O-GlcNAc) glycosylation (O-GlcNAcylation) in AMPA receptor trafficking. Alloxan, an inhibitor of O-GlcNAc transferase, potentiated responses of AMPA receptors composed of the GluR1 subunit expressed in Xenopus oocytes. No potentiating effect of alloxan was obtained with mutant GluR1 (S831A) receptor lacking CaMKII phosphorylation site. Alloxan facilitated basal synaptic transmission to approximately 120% of basal levels and enhanced Schaffer collateral-CA1 long-term potentiation (LTP) in rat hippocampal slices, especially in the late phase of the LTP. Alloxan stimulated translocation of the GluR1 and GluR2 subunit from the cytosol towards the plasma membrane in rat hippocampal slices with the LTP, although it had no effect on subcellular distribution of the NR1 subunit. Taken together, the results of the present study show that alloxan regulates AMPA receptor trafficking by inhibiting O-GlcNAcylation, to modulate hippocampal synaptic transmission and synaptic plasticity.

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CRRD Object Information
CRRD ID: 4107350
Created: 2010-07-15
Species: All species
Last Modified: 2010-07-15
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.