Chapter

Molecular Organization of Glutamate Receptors in the Postsynaptic Density

ROBERT BALÁZS, RICHARD J. BRIDGES and CARL W. COTMAN

in Excitatory Amino Acid Transmission in Health and Disease

Published in print October 2005 | ISBN: 9780195150025
Published online January 2010 | e-ISBN: 9780199865079 | DOI: http://dx.doi.org/10.1093/acprof:oso/9780195150025.003.0009
Molecular Organization of Glutamate Receptors in the Postsynaptic Density

Show Summary Details

Preview

A significant advance in the field of excitatory amino acid (EAA) transmission has been the great progress made toward elucidation of the molecular composition and function of the postsynaptic density (PSD) complex, one of the defining structural features of excitatory synapses. The PSD complex is a marked thickening localized to the postsynaptic side of asymmetric, excitatory synapses and consists of a network of scaffolding, cytoskeletal, and regulatory proteins in association with ionotropic glutamate receptors (iGluRs) and some of the metabotropic glutamate receptors (mGluRs). Biochemical and immunocytochemical characterization showed that, among its constituent proteins, N-methyl-D-aspartate (NMDA) receptors are highly represented compared with the other EAA receptors, reflecting the fact that they are the most tightly integrated receptors within the complex. This chapter looks at the molecular organization of glutamate receptors in the PSD complex, NMDA receptors within the PSD complex, AMPA receptors within the PSD complex, kainate receptors within the PSD complex, and mGluRs within the PSD complex.

Keywords: glutamate receptors; postsynaptic density; excitatory amino acids; excitatory synapses; kainate receptors; AMPA receptors; NMDA receptors; metabotropic glutamate receptors

Chapter.  6904 words.  Illustrated.

Subjects: Neuroscience

Full text: subscription required

How to subscribe Recommend to my Librarian

Buy this work at Oxford University Press »

Users without a subscription are not able to see the full content. Please, subscribe or login to access all content.