Crystal structure and association behaviour of the GluR2 amino-terminal domain

Authors

  • Rongsheng Jin,

    Corresponding author
    1. Center for Neuroscience, Aging, and Stem Cell Research, Burnham Institute for Medical Research, La Jolla, CA, USA
    2. These authors contributed equally to this work
    • Corresponding authors. Vollum Institute, Howard Hughes Medical Institute, Oregon Health and Science University, Portland, OR 97239, USA. Tel.: +1 503 494 55 35; Fax: +1 503 494 17 00; E-mail: rjin@burnham.org or E-mail: gouauxe@ohsu.edu

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  • Satinder K Singh,

    1. Vollum Institute, Oregon Health and Science University, Portland, OR, USA
    2. These authors contributed equally to this work
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  • Shenyan Gu,

    1. Center for Neuroscience, Aging, and Stem Cell Research, Burnham Institute for Medical Research, La Jolla, CA, USA
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  • Hiroyasu Furukawa,

    1. Vollum Institute, Oregon Health and Science University, Portland, OR, USA
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  • Alexander I Sobolevsky,

    1. Vollum Institute, Oregon Health and Science University, Portland, OR, USA
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  • Jie Zhou,

    1. Center for Neuroscience, Aging, and Stem Cell Research, Burnham Institute for Medical Research, La Jolla, CA, USA
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  • Yan Jin,

    1. Department of Biochemistry and Molecular Biophysics, Howard Hughes Medical Institute, Columbia University, New York, NY, USA
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  • Eric Gouaux

    Corresponding author
    1. Vollum Institute, Oregon Health and Science University, Portland, OR, USA
    2. Howard Hughes Medical Institute, Oregon Health and Science University, Portland, OR, USA
    • Corresponding authors. Vollum Institute, Howard Hughes Medical Institute, Oregon Health and Science University, Portland, OR 97239, USA. Tel.: +1 503 494 55 35; Fax: +1 503 494 17 00; E-mail: rjin@burnham.org or E-mail: gouauxe@ohsu.edu

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Abstract

Fast excitatory neurotransmission is mediated largely by ionotropic glutamate receptors (iGluRs), tetrameric, ligand-gated ion channel proteins comprised of three subfamilies, AMPA, kainate and NMDA receptors, with each subfamily sharing a common, modular-domain architecture. For all receptor subfamilies, active channels are exclusively formed by assemblages of subunits within the same subfamily, a molecular process principally encoded by the amino-terminal domain (ATD). However, the molecular basis by which the ATD guides subfamily-specific receptor assembly is not known. Here we show that AMPA receptor GluR1- and GluR2-ATDs form tightly associated dimers and, by the analysis of crystal structures of the GluR2-ATD, propose mechanisms by which the ATD guides subfamily-specific receptor assembly.

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