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Molecular determinants for the interaction between AMPA receptors and the clathrin adaptor complex AP-2.

Authors: Kastning, Kathrin  Kukhtina, Viktoria  Kittler, Josef T  Chen, Guojun  Pechstein, Arndt  Enders, Sven  Lee, Sang Hyoung  Sheng, Morgan  Yan, Zhen  Haucke, Volker 
Citation: Kastning K, etal., Proc Natl Acad Sci U S A. 2007 Feb 20;104(8):2991-6. Epub 2007 Feb 8.
Pubmed: (View Article at PubMed) PMID:17289840
DOI: Full-text: DOI:10.1073/pnas.0611170104

alpha-Amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA)-type glutamate receptors undergo constitutive and ligand-induced internalization that requires dynamin and the clathrin adaptor complex AP-2. We report here that an atypical basic motif within the cytoplasmic tails of AMPA-type glutamate receptors directly associates with mu2-adaptin by a mechanism similar to the recognition of the presynaptic vesicle protein synaptotagmin 1 by AP-2. A synaptotagmin 1-derived AP-2 binding peptide competes the interaction of the AMPA receptor subunit GluR2 with AP-2mu and increases the number of surface active glutamate receptors in living neurons. Moreover, fusion of the GluR2-derived tail peptide with a synaptotagmin 1 truncation mutant restores clathrin/AP-2-dependent internalization of the chimeric reporter protein. These data suggest that common mechanisms regulate AP-2-dependent internalization of pre- and postsynaptic membrane proteins.

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CRRD Object Information
CRRD ID: 13432317
Created: 2017-09-26
Species: All species
Last Modified: 2017-09-26
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.