Abstract:
: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.
journal_name
Proc Natl Acad Sci U S Aauthors
Kastning K,Kukhtina V,Kittler JT,Chen G,Pechstein A,Enders S,Lee SH,Sheng M,Yan Z,Haucke Vdoi
10.1073/pnas.0611170104subject
Has Abstractpub_date
2007-02-20 00:00:00pages
2991-6issue
8eissn
0027-8424issn
1091-6490pii
0611170104journal_volume
104pub_type
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