Mutagenesis Reveals a Role for ABP/GRIP Binding to GluR2 in Synaptic Surface Accumulation of the AMPA Receptor
@article{Osten2000MutagenesisRA, title={Mutagenesis Reveals a Role for ABP/GRIP Binding to GluR2 in Synaptic Surface Accumulation of the AMPA Receptor}, author={Pavel Osten and Latika Khatri and J. L. Beato P{\'e}rez and Georg K{\"o}hr and Guenter Giese and Christopher Daly and Torsten W. Schulz and Allen K. Wensky and Laveria M Lee and Edward Benjamin Ziff}, journal={Neuron}, year={2000}, volume={27}, pages={313-325} }
315 Citations
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References
SHOWING 1-10 OF 96 REFERENCES
Novel Anchorage of GluR2/3 to the Postsynaptic Density by the AMPA Receptor–Binding Protein ABP
- Biology, ChemistryNeuron
- 1998
Characterization of the Glutamate Receptor-Interacting Proteins GRIP1 and GRIP2
- BiologyThe Journal of Neuroscience
- 1999
Results suggest that GRIP1 and GRIP2 are AMPA receptor binding proteins potentially involved in the targeting of AMPA receptors to synapses, as well as in early neuronal development.
Association of AMPA Receptors with a Subset of Glutamate Receptor-Interacting Protein In Vivo
- Biology, ChemistryThe Journal of Neuroscience
- 1999
Findings support a role for GRIP in the synaptic anchoring of AMPA receptors but also suggest that GRIP has additional functions unrelated to the binding of AMpa receptors.
GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors
- BiologyNature
- 1997
GRIP is a new member of the PDZ domain-containing protein family which has seven PDZ domains and no catalytic domain and appears to serve as an adapter protein that links AMPA receptors to other proteins and may be critical for the clustering of AMPA receptor at excitatory synapses in the brain.
Hippocampal LTD Expression Involves a Pool of AMPARs Regulated by the NSF–GluR2 Interaction
- BiologyNeuron
- 1999
Essential Role for dlg in Synaptic Clustering of Shaker K+ Channels In Vivo
- BiologyThe Journal of Neuroscience
- 1997
It is demonstrated for the first time that DLG plays an important role in synaptic organization in vivo that correlates with its ability to bind directly to specific membrane proteins of the synapse.