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Resources » Paper

Howard Chang et al. (2002) East Coast Worm Meeting "Functional analysis of AMPA-type glutamate receptor cytosolic tail sequences and their contribution to receptor localization at synapses"

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  • Comments on Howard Chang et al. (2002) East Coast Worm Meeting "Functional analysis of AMPA-type glutamate receptor cytosolic tail sequences and their contribution to receptor localization at synapses" (0)

  • Overview

    Status:
    Publication type:
    Meeting_abstract
    WormBase ID:
    WBPaper00010379

    Howard Chang, & Christopher Rongo (2002). Functional analysis of AMPA-type glutamate receptor cytosolic tail sequences and their contribution to receptor localization at synapses presented in East Coast Worm Meeting. Unpublished information; cite only with author permission.

    The modulation of AMPA-type glutamate receptor localization to central nervous system synapses is an important component of synaptic plasticity, and can be triggered by LTP (Long Term Potentiation) and CaMKII (Type II calcium-calmodulin-dependent protein kinase) activity. (1, 2). In mammalian hippocampal neurons, the different AMPA receptor subunits GluR1, GluR2, GluR3, and GluR4 are proposed to form heteromultimers, and individual subunits can confer localization specificity to the multimeric channels that they comprise (2,3). One likely explanation for such subunit specificity is that the targeting of AMPA receptors to the synapses is probably due to the interaction of PDZ domain-containing proteins and the receptor subunit cytosolic tail sequences (4). In C. elegans, there are four AMPA receptor subunits that are expressed in the command interneurons, including, glr-1, glr-2, glr-4 and glr-5 (5). We are using the molecular, genetic, and cell biological approaches to examine the delivering of AMPA receptors. We hope to identify the PDZ domain-containing proteins that interact with the tail sequences of AMPA receptors in C. elegans in order to understand the localization and regulation of these receptors in response to plasticity at synapses.


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