The AMPA receptor GluR2 C terminus can mediate a reversible, ATP- dependent interaction with NSF and α- and β-SNAPs

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, 21 (1). pp. 99-110. ISSN 08966273 (ISSN)

URL: http://www.ncbi.nlm.nih.gov/pubmed/9697855
DOI: 10.1016/s0896-6273(00)80518-8

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: Paper
Uncontrolled Keywords: AMPA receptor synaptosomal associated protein 25 article carboxy terminal sequence extracellular matrix hydrolysis mediator release membrane fusion nonhuman priority journal protein domain protein localization protein processing protein protein interaction RNA editing synaptic transmission Adenosine Triphosphate Amino Acid Sequence Animals Carrier Proteins Dendrites Drug Interactions Membrane Proteins N-Ethylmaleimide-Sensitive Proteins Neurons Precipitation Qa-SNARE Proteins Rats Rats, Sprague-Dawley Receptors, AMPA Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins Vesicular Transport Proteins Yeasts
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > AMPA receptor
bioinformatics > genomics and proteomics > genetics & nucleic acid processing
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > SNAP protein
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Osten lab
Depositing User: Matt Covey
Date: 1998
Date Deposited: 04 Apr 2013 21:12
Last Modified: 04 Apr 2013 21:12
Related URLs:
URI: http://repository.cshl.edu/id/eprint/28094

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving