Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphate / analogs & derivatives
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Adenosine Triphosphate / pharmacology
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Adenosine Triphosphate / physiology*
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Amino Acid Sequence
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Animals
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Carrier Proteins / physiology*
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Chemical Precipitation
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Dendrites / metabolism
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Drug Interactions
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Membrane Proteins / physiology*
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N-Ethylmaleimide-Sensitive Proteins
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Neurons / metabolism
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Qa-SNARE Proteins
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Rats
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Rats, Sprague-Dawley
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Receptors, AMPA / physiology*
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Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
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Vesicular Transport Proteins*
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Yeasts / genetics
Substances
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Carrier Proteins
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Membrane Proteins
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Qa-SNARE Proteins
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Receptors, AMPA
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Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
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Vesicular Transport Proteins
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adenosine 5'-O-(3-thiotriphosphate)
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Adenosine Triphosphate
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N-Ethylmaleimide-Sensitive Proteins
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Nsf protein, rat
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glutamate receptor ionotropic, AMPA 2