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

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.

authors

Kastning K,Kukhtina V,Kittler JT,Chen G,Pechstein A,Enders S,Lee SH,Sheng M,Yan Z,Haucke V

doi

10.1073/pnas.0611170104

subject

Has Abstract

pub_date

2007-02-20 00:00:00

pages

2991-6

issue

8

eissn

0027-8424

issn

1091-6490

pii

0611170104

journal_volume

104

pub_type

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