http://www.cnr.it/ontology/cnr/individuo/prodotto/ID38150

Extracellular interactions between GluR2 and N-cadherin in spine regulation. (Articolo in rivista)

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Extracellular interactions between GluR2 and N-cadherin in spine regulation. (Articolo in rivista) (literal)

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Alternative label

Saglietti L, Dequidt C, Kamieniarz K, Rousset MC, Valnegri P, Thoumine O, Beretta F, Fagni L, Choquet D, Sala C, Sheng M and Passafaro M (2007)
Extracellular interactions between GluR2 and N-cadherin in spine regulation.
in Neuron (Camb. Mass.)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Saglietti L, Dequidt C, Kamieniarz K, Rousset MC, Valnegri P, Thoumine O, Beretta F, Fagni L, Choquet D, Sala C, Sheng M and Passafaro M (literal)

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1)DTI Dulbecco Telethon Institute, CNR Institute of Neuroscience, Cellular and Molecular Pharmacology, Department of Pharmacology, University of Milan, Italy 2)CNRS, UMR 5091, Institute Magendie de Neurosciences, Universite` Bordeaux, France 3 )Institut de Ge´ nomique Fonctionnelle, Unite´ Mixte de Recherche 5203, 34000 Montpellier, France 4)CNR Institute of Neuroscience, Cellular and Molecular Pharmacology, Department of Pharmacology, University of Milan, Italy 5)The Picower Institute for Learning and Memory, RIKEN-MIT Neuroscience Research Center, Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA 02139, USA 6)Present address: Department of Molecular Virology, Institute of Experimental Biology, Umultowska, Poznan, Poland. (literal)

Titolo

Extracellular interactions between GluR2 and N-cadherin in spine regulation. (literal)

Abstract

Via its extracellular N-terminal domain (NTD), theAMPA receptor subunit GluR2 promotes the formation and growth of dendritic spines in cultured hippocampal neurons. Here we show that the first N-terminal 92 amino acids of the extracellular domain are necessary and sufficient for GluR20s spine-promoting activity. Moreover, overexpression of this extracellular domain increases the frequency of miniature excitatory postsynaptic currents (mEPSCs). Biochemically, the NTD of GluR2 can interact directly with the cell adhesion molecule N-cadherin, in cis or in trans. N-cadherin-coated beads recruit GluR2 on the surface of hippocampal neurons, and N-cadherin immobilization decreases GluR2 lateral diffusion on the neuronal surface. RNAi knockdown of N-cadherin prevents the enhancing effect of GluR2 on spine morphogenesis and mEPSC frequency. Our data indicate that in hippocampal neurons N-cadherin and GluR2 form a synaptic complex that stimulates presynaptic development and function as well as promoting dendritic spine formation. (literal)

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