Literature DB >> 16980545

Two mutations preventing PDZ-protein interactions of GluR1 have opposite effects on synaptic plasticity.

Jannic Boehm1, Ingrid Ehrlich, Helen Hsieh, Roberto Malinow.   

Abstract

The regulated trafficking of GluR1 contributes significantly to synaptic plasticity, but studies addressing the function of the GluR1 C-terminal PDZ-ligand domain in this process have produced conflicting results. Here, we resolve this conflict by showing that apparently similar C-terminal mutations of the GluR1 PDZ-ligand domain result in opposite physiological phenotypes during activity- and CamKII-induced synaptic plasticity.

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Year:  2006        PMID: 16980545     DOI: 10.1101/lm.253506

Source DB:  PubMed          Journal:  Learn Mem        ISSN: 1072-0502            Impact factor:   2.460


  13 in total

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10.  Analysis of the potential role of GluA4 carboxyl-terminus in PDZ interactions.

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