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The Journal of Neuroscience, September 29, 2004, 24(39):8584-8594; doi:10.1523/JNEUROSCI.2100-04.2004

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Cellular/Molecular
Actin/-Actinin-Dependent Transport of AMPA Receptors in Dendritic Spines: Role of the PDZ-LIM Protein RIL

Torsten W. Schulz,^1 * Terunaga Nakagawa,^2 * Pawel Licznerski,^1 * Verena Pawlak,^1 * Alexander Kolleker,¹ Andrei Rozov,¹ Jinhyun Kim,¹ Tanjew Dittgen,¹ Georg Köhr,¹ Morgan Sheng,² Peter H. Seeburg,¹ and Pavel Osten¹

¹Max Planck Institute for Medical Research, Department of Molecular Neurobiology, 69120 Heidelberg, Germany, ²The Picower Center for Learning and Memory, Howard Hughes Medical Institute, RIKEN-MIT Neuroscience Research Center, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139-4307

The efficacy of excitatory transmission in the brain depends to a large extent on synaptic AMPA receptors, hence the importance of understanding the delivery and recycling of the receptors at the synaptic sites. Here we report a novel regulation of the AMPA receptor transport by a PDZ (postsynaptic density-95/Drosophila disc large tumor suppressor zona occludens 1) and LIM (Lin11/rat Isl-1/Mec3) domain-containing protein, RIL (reversion-induced LIM protein). We show that RIL binds to the AMPA glutamate receptor subunit GluR-A C-terminal peptide via its LIM domain and to -actinin via its PDZ domain. RIL is enriched in the postsynaptic density fraction isolated from rat forebrain, strongly localizes to dendritic spines in cultured neurons, and coprecipitates, together with -actinin, in a protein complex isolated by immunoprecipitation of AMPA receptors from forebrain synaptosomes. Functionally, in heterologous cells, RIL links AMPA receptors to the -actinin/actin cytoskeleton, an effect that appears to apply selectively to the endosomal surface-internalized population of the receptors. In cultured neurons, an overexpression of recombinant RIL increases the accumulation of AMPA receptors in dendritic spines, both at the total level, as assessed by immunodetection of endogenous GluR-A-containing receptors, and at the synaptic surface, as assessed by recording of miniature EPSCs. Our results thus indicate that RIL directs the transport of GluR-A-containing AMPA receptors to and/or within dendritic spines, in an-actinin/actin-dependent manner, and that such trafficking function promotes the synaptic accumulation of the receptors.

Key words: AMPA receptor; transport; dendritic spine; -actinin/actin cytoskeleton; PDZ domain; LIM domain

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Received May 31, 2004; revised August 17, 2004; accepted August 17, 2004.

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