Dynamic regulation of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs) underlies aspects of synaptic plasticity. Although numerous AMPAR-interacting proteins have been identified, their quantitative and relative contributions to native AMPAR complexes remain unclear. Here, we quantitated protein interactions with neuronal AMPARs by immunoprecipitation from brain extracts. We found that stargazin-like transmembrane AMPAR regulatory proteins (TARPs) copurified with neuronal AMPARs, but we found negligible binding to GRIP, PICK1, NSF, or SAP-97. To facilitate purification of neuronal AMPAR complexes, we generated a transgenic mouse expressing an epitope-tagged GluR2 subunit of AMPARs. Taking advantage of this powerful new tool, we isolated two populations of GluR2 containing AMPARs: an immature complex with the endoplasmic reticulum chaperone immunoglobulin-binding protein and a mature complex containing GluR1, TARPs, and PSD-95. These studies establish TARPs as the auxiliary components of neuronal AMPARs.
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9 May 2005
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May 09 2005
Molecular constituents of neuronal AMPA receptors
Yuko Fukata,
Yuko Fukata
1Department of Physiology, University of California, San Francisco, San Francisco, CA 94143
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Anastassios V. Tzingounis,
Anastassios V. Tzingounis
2Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94143
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Jonathan C. Trinidad,
Jonathan C. Trinidad
3Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143
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Masaki Fukata,
Masaki Fukata
1Department of Physiology, University of California, San Francisco, San Francisco, CA 94143
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Alma L. Burlingame,
Alma L. Burlingame
3Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143
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Roger A. Nicoll,
Roger A. Nicoll
2Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94143
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David S. Bredt
David S. Bredt
1Department of Physiology, University of California, San Francisco, San Francisco, CA 94143
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Yuko Fukata
1Department of Physiology, University of California, San Francisco, San Francisco, CA 94143
Anastassios V. Tzingounis
2Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94143
Jonathan C. Trinidad
3Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143
Masaki Fukata
1Department of Physiology, University of California, San Francisco, San Francisco, CA 94143
Alma L. Burlingame
3Department of Pharmaceutical Chemistry, University of California, San Francisco, San Francisco, CA 94143
Roger A. Nicoll
2Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94143
David S. Bredt
1Department of Physiology, University of California, San Francisco, San Francisco, CA 94143
Correspondence to David S. Bredt: [email protected]
Y. Fukata and M. Fukata's present address is Laboratory of Genomics and Proteomics, National Institute for Longevity Sciences, Obu, Aichi 474-8522, Japan.
Abbreviations used in this paper: AMPA, α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid; AMPAR, AMPA receptor; CBP, calmodulin-binding peptide; IAP, immunoaffinity purification; LTD, long-term depression; NMDA, N-methyl-d-aspartate; TARP, transmembrane AMPAR regulatory protein.
Received:
January 24 2005
Accepted:
March 31 2005
Online ISSN: 1540-8140
Print ISSN: 0021-9525
The Rockefeller University Press
2005
J Cell Biol (2005) 169 (3): 399–404.
Article history
Received:
January 24 2005
Accepted:
March 31 2005
Citation
Yuko Fukata, Anastassios V. Tzingounis, Jonathan C. Trinidad, Masaki Fukata, Alma L. Burlingame, Roger A. Nicoll, David S. Bredt; Molecular constituents of neuronal AMPA receptors . J Cell Biol 9 May 2005; 169 (3): 399–404. doi: https://doi.org/10.1083/jcb.200501121
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