The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
The AMPA Receptor GluR2 C Terminus Can Mediate a Reversible, ATP-Dependent Interaction with NSF and α- and β-SNAPs
Open accessAbstract
In this study, we demonstrate specific interaction of the GluR2 alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) receptor subunit C-terminal peptide with an ATPase N-ethylmaleimide-sensitive fusion protein (NSF) and alpha- and beta-soluble NSF attachment proteins (SNAPs), as well as dendritic colocalization of these proteins. The assembly of the GluR2-NSF-SNAP complex is ATP hydrolysis reversible and resembles the binding of NSF and SNAP with the SNAP receptor (SNARE) membrane fusion apparatus. We provide evidence that the molar ratio of NSF to SNAP in the GluR2-NSF-SNAP complex is similar to that of the t-SNARE syntaxin-NSF-SNAP complex. NSF is known to disassemble the SNARE protein complex in a chaperone-like interaction driven by ATP hydrolysis. We propose a model in which NSF functions as a chaperone in the molecular processing of the AMPA receptor.
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Cites
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Cited by
Glutamate Receptor Ion Channels: Structure, Regulation, and Function
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AMPA receptor trafficking at excitatory synapses
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Metadata
- Authors
- Osten, P., Srivastava, S., Inman, G. J., Vilim, F. S., Khatri, L., Lee, L. M., States, B. A., Einheber, S., Milner, T. A., Hanson, P. I., & Ziff, E. B.
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1998-07
- Volume
- 21
- Issue
- 1
- Pages
- 99-110
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2148156937
- Cited by
- 357
- References
- 42
- FWCI
- 13.69
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Osten, P., Srivastava, S., Inman, G. J., Vilim, F. S., Khatri, L., Lee, L. M., States, B. A., Einheber, S., Milner, T. A., Hanson, P. I., & Ziff, E. B. (1998). The AMPA Receptor GluR2 C Terminus Can Mediate a Reversible, ATP-Dependent Interaction with NSF and α- and β-SNAPs. Neuron. https://doi.org/10.1016/s0896-6273(00)80518-8
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