Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 104, Issue 8, Pages 2991-2996Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0611170104
Keywords
endocytosis; postsynaptic; sorting signal; synaptic plasticity
Categories
Funding
- MRC [G120/972] Funding Source: UKRI
- Medical Research Council [G120/972] Funding Source: Medline
- Medical Research Council [G120/972] Funding Source: researchfish
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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 mu 2-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-2 mu 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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