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Journal Article

Mutagenesis reveals a role for ABP/GRIP binding to GluR2 in synaptic surface accumulation of the AMPA receptor

MPS-Authors
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Osten,  Pavel
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Köhr,  Georg
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

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Giese,  Günter
Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society;

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Schulz,  Torsten Wilhelm
Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society;

External Resource

http://www.sciencedirect.com/science/article/pii/S0896627300000398/pdfft?md5=a6b8336efecb2e5a8f42cbe3ed7596a3&pid=1-s2.0-S0896627300000398-main.pdf
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http://dx.doi.org/10.1016/S0896-6273(00)00039-8
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Citation

Osten, P., Khatri, L., Perez, J. L., Köhr, G., Giese, G., Daly, C., et al. (2000). Mutagenesis reveals a role for ABP/GRIP binding to GluR2 in synaptic surface accumulation of the AMPA receptor. Neuron, 27, 313-325. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/10985351.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-2D37-C
Abstract
We studied the role of PDZ proteins GRIP, ABP, and PICK1 in GluR2 AMPA receptor trafficking. An epitope-tagged MycGluR2 subunit, when expressed in hippocampal cultured neurons, was specifically targeted to the synaptic surface. With the mutant MycGluR2?1-10, which lacks the PDZ binding site, the overall dendritic intracellular transport and the synaptic surface targeting were not affected. However, over time, MycGluR2?1-10 accumulated at synapses significantly less than MycGluR2. Notably, a single residue substitution, S880A, which blocks binding to ABP/GRIP but not to PICK1, reduced synaptic accumulation to the same extent as the PDZ site truncation. We conclude that the association of GluR2 with ABP and/or GRIP but not PICK1 is essential for maintaining the synaptic surface accumulation of the receptor, possibly by limiting its endocytotic rate