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Cytoskeletal protein 4.1G is a binding partner of the metabotropic glutamate receptor subtype 1α
Author(s) -
Lu Dongcheng,
Yan Henglin,
Othman Timothy,
Rivkees Scott A.
Publication year - 2004
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.20230
Subject(s) - metabotropic glutamate receptor , metabotropic receptor , glutamate receptor , metabotropic glutamate receptor 1 , microbiology and biotechnology , cytoskeleton , metabotropic glutamate receptor 5 , hek 293 cells , metabotropic glutamate receptor 6 , metabotropic glutamate receptor 2 , biology , chemistry , hippocampal formation , receptor , biochemistry , neuroscience , cell
Recent evidence suggests that cytoskeletal proteins play important roles in the clustering and anchoring of glutamate receptors to the cell surface membrane. To examine further this issue, we tested for direct interactions between the metabotropic glutamate receptor subtype 1α (mGlu1α) and 4.1G, which is a member of the erythrocyte membrane, cytoskeletal protein 4.1 family. First, co‐localization of 4.1G and mGlu1α was observed in cultured hippocampal neurons. Second, in transiently transfected HEK 293 cells and in whole rat brain tissue, direct interactions between mGlu1α and 4.1G were observed. Third, we were able to identify the C‐terminal tail of mGlu1α as an essential region for mGlu1α–4.1G interactions. Fourth, 4.1 G influences mGlu1α‐mediated cAMP accumulation. Finally, we found that 4.1G increases the ligand‐binding ability of mGlu1α and alters its cellular distribution. These observations identify 4.1G as a novel binding partner of mGlu1α that can regulate the action of mGlu1α. © 2004 Wiley‐Liss, Inc.