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Stargazin Is an AMPA Receptor Auxiliary Subunit
Wim Vandenberghe, Roger A. Nicoll and David S. Bredt
Proceedings of the National Academy of Sciences of the United States of America
Vol. 102, No. 2 (Jan. 11, 2005), pp. 485-490
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/3374271
Page Count: 6
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AMPA (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptors mediate fast excitatory synaptic transmission in brain and underlie aspects of synaptic plasticity. Numerous AMPA receptor-binding proteins have been implicated in AMPA receptor trafficking and anchoring. However, the relative contributions of these proteins to the composition of native AMPA receptor complexes in brain remain uncertain. Here, we use blue native gel electrophoresis to analyze the composition of native AMPA receptor complexes in cerebellar extracts. We identify two receptor populations: a functional form that contains the transmembrane AMPA receptor-regulatory protein stargazin and an apo-form that lacks stargazin. Limited proteolysis confirms assembly of stargazin with a large proportion of native AMPA receptors. In contrast, other AMPA receptor-interacting proteins, such as synapse-associated protein 97, glutamate receptor-interacting protein 1, protein kinase Cα binding protein, N-ethylmaleimide-sensitive fusion protein, AP2, and protein 4. 1N, do not show significant association with AMPA receptor complexes on native gels. These data identify stargazin as an auxiliary subunit for a neurotransmitter-gated ion channel.
Proceedings of the National Academy of Sciences of the United States of America © 2005 National Academy of Sciences