Osten, P. et al. (1998) The AMPA receptor GluR2 C terminus can mediate a reversible, ATP-dependent interaction with NSF and α- and β-SNAPs. Neuron, 21(1), pp. 99-110. (doi: 10.1016/s0896-6273(00)80518-8) (PMID:9697855)
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Abstract
In this study, we demonstrate specific interaction of the GluR2 α-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) receptor subunit C-terminal peptide with an ATPase N-ethylmaleimide–sensitive fusion protein (NSF) and α- and β-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.
Item Type: | Articles |
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Additional Information: | S. S. was supported by National Institutes of Health grant AG13620 (to E. B. Z.). P. I. H. was supported by a postdoctoral fellowship from the Helen Hay Whitney Foundation. S. E. was supported by a grant from the Epilepsy Foundation of America. T. A. M. was supported by National Institutes of Health grant MH42834. P. O., G. J. I., and F. S. V. are Associates and E. B. Z. an Investigator of the Howard Hughes Medical Institute. |
Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Inman, Professor Gareth |
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., and Ziff, E.B. |
College/School: | College of Medical Veterinary and Life Sciences > School of Cancer Sciences |
Journal Name: | Neuron |
Publisher: | Elsevier |
ISSN: | 0896-6273 |
ISSN (Online): | 1097-4199 |
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