Molecular determinants for the interaction between AMPA receptors and the clathrin adaptor complex AP-2. Proc Natl Acad Sci U S A 2007 Feb 20;104(8):2991-6
Date
02/10/2007Pubmed ID
17289840Pubmed Central ID
PMC1815294DOI
10.1073/pnas.0611170104Scopus ID
2-s2.0-33847321605 (requires institutional sign-in at Scopus site) 80 CitationsAbstract
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.
Author List
Kastning K, Kukhtina V, Kittler JT, Chen G, Pechstein A, Enders S, Lee SH, Sheng M, Yan Z, Haucke VAuthor
Sang H. Lee PhD Professor in the Pharmacology and Toxicology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Adaptor Protein Complex mu SubunitsAmino Acid Motifs
Amino Acid Sequence
Amino Acids, Basic
Animals
COS Cells
Cell Survival
Clathrin
Endocytosis
Excitatory Postsynaptic Potentials
Humans
Molecular Sequence Data
Neurons
Peptides
Protein Binding
Rats
Receptors, AMPA
Recombinant Fusion Proteins
Synaptic Vesicles
Synaptotagmin I
