Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms

Lu Chen, Dane M. Chetkovich, Ronald S. Petralia, Neal T. Sweeney, Yoshimi Kawasaki, Robert J. Wenthold, David S. Bredt and Roger A. Nicoll ()
Additional contact information
Lu Chen: Cellular and Molecular Pharmacology,
Dane M. Chetkovich: Departments of Physiology
Ronald S. Petralia: Laboratory of Neurochemistry, NIDCD, National Institutes of Health
Neal T. Sweeney: Departments of Physiology
Yoshimi Kawasaki: Departments of Physiology
Robert J. Wenthold: Laboratory of Neurochemistry, NIDCD, National Institutes of Health
David S. Bredt: Departments of Physiology
Roger A. Nicoll: Cellular and Molecular Pharmacology,

Nature, 2000, vol. 408, issue 6815, 936-943

Abstract: Abstract Stargazer, an ataxic and epileptic mutant mouse, lacks functional AMPA (α-amino-3-hydroxyl-5-methyl-4-isoxazolepropionate) receptors on cerebellar granule cells. Stargazin, the mutated protein, interacts with both AMPA receptor subunits and synaptic PDZ proteins, such as PSD-95. The interaction of stargazin with AMPA receptor subunits is essential for delivering functional receptors to the surface membrane of granule cells, whereas its binding with PSD-95 and related PDZ proteins through a carboxy-terminal PDZ-binding domain is required for targeting the AMPA receptor to synapses. Expression of a mutant stargazin lacking the PDZ-binding domain in hippocampal pyramidal cells disrupts synaptic AMPA receptors, indicating that stargazin-like mechanisms for targeting AMPA receptors may be widespread in the central nervous system.

Date: 2000
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DOI: 10.1038/35050030

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