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  Fe65 interacts with P2X₂ subunits at excitatory synapses and modulates receptor function

Masin, M., Kerschensteiner, D., Dümke, K., Rubio, M. E., & Soto, F. (2006). Fe65 interacts with P2X₂ subunits at excitatory synapses and modulates receptor function. Journal of Biological Chemistry, 281(7), 4100-4108.

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 Creators:
Masin, Marianela1, Author           
Kerschensteiner, Daniel1, Author           
Dümke, Kerstin1, Author           
Rubio, Maria E., Author
Soto, Florentina1, Author           
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1Molecular biology of neuronal signals, Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173656              

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Free keywords: AMYLOID PRECURSOR PROTEIN; PHOSPHOTYROSINE-BINDING DOMAIN; PROLINE-RICH MOTIFS; GATED ION CHANNELS; ADAPTER PROTEIN; C-TERMINUS; IONOTROPIC RECEPTOR; CYTOPLASMIC DOMAIN; SIGNALING PROTEINS; ATP RECEPTOR
 Abstract: Ionotropic receptors in the neuronal plasmamembrane are organized in macromolecular complexes, which assure their proper localization and regulate signal transduction. P2X receptors, the ionotropic receptors activated by extracellular ATP, have been shown to influence synaptic transmission. Using a yeast two-hybrid approach with the P2X(2) subunit C-terminal domain as bait we isolated the beta-amyloid precursor protein-binding proteins Fe65 and Fe65-like 1 as the first identified proteins interacting with neuronal P2X receptors. We confirmed the direct interaction of Fe65 and the P2X(2) C-terminal domain by glutathione S-transferase pull-down experiments. No interaction was observed between Fe65 and the naturally occurring P2X(2) splice variant P2X(2(b)), indicating that alternative splicing can regulate the receptor complex assembly. We generated two antibodies to Fe65 to determine its subcellular localization using postembedding immunogold labeling electron microscopy. We found labeling for Fe65 at the pre- and postsynaptic specialization of CA1 hippocampal pyramidal cell/Schaffer collateral synapses. By double immunogold labeling, we determined that Fe65 colocalizes with P2X(2) subunits at the postsynaptic specialization of excitatory synapses. Moreover, P2X(2) and Fe65 could be coimmunoprecipitated from brain membrane extracts, demonstrating that the interaction occurs in vivo. The assembly with Fe65 regulates the functional properties of P2X(2) receptors. Thus, the time- and activation-dependent change in ionic selectivity of P2X(2) receptors was inhibited by coexpression of Fe65, suggesting a novel role for Fe65 in regulating P2X receptor function and ATP-mediated synaptic transmission.

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Language(s): eng - English
 Dates: 2006-02
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 292199
ISI: 000235275300040
ISI: 000235275300040
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Title: Journal of Biological Chemistry
  Alternative Title : J.Biol.Chem.
Source Genre: Journal
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Pages: - Volume / Issue: 281 (7) Sequence Number: - Start / End Page: 4100 - 4108 Identifier: ISSN: 0021-9258