GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors

Hualing Dong, Richard J. O'Brien, Eric T. Fung, Anthony A. Lanahan, Paul F. Worley and Richard L. Huganir
Additional contact information
Hualing Dong: Johns Hopkins University School of Medicine
Richard J. O'Brien: Johns Hopkins University School of Medicine
Eric T. Fung: Johns Hopkins University School of Medicine
Anthony A. Lanahan: Johns Hopkins University School of Medicine
Paul F. Worley: Johns Hopkins University School of Medicine
Richard L. Huganir: Johns Hopkins University School of Medicine

Nature, 1997, vol. 386, issue 6622, 279-284

Abstract: Abstract AMPA glutamate receptors mediate the majority of rapid excitatory synaptic transmission in the central nervous system1,2 and play a role in the synaptic plasticity underlying learning and memory3,4. AMPA receptors are heteromeric complexes of four homologous subunits (GluRl–4) that differentially combine to form a variety of AMPA receptor subtypes1,2. These subunits are thought to have a large extracellular amino-terminal domain, three transmembrane domains and an intracellular carboxy-terminal domain5. AMPA receptors are localized at excitatory synapses and are not found on adjacent inhibitory synapses enriched in GABAA receptors6. The targeting of neurotransmitter receptors, such as AMPA receptors, and ion channels to synapses is essential for efficient transmission7,8. A protein motif called a PDZ domain is important in the targeting of a variety of membrane proteins to cell–cell junctions including synapses8–10. Here we identify a synaptic PDZ domain-containing protein GRIP (glutamate receptor interacting protein) that specifically interacts with the C termini of AMPA receptors. GRIP is a new member of the PDZ domain-containing protein family which has seven PDZ domains and no catalytic domain. GRIP appears to serve as an adapter protein that links AMPA receptors to other proteins and may be critical for the clustering of AMPA receptors at excitatory synapses in the brain.

Date: 1997
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/386279a0 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:386:y:1997:i:6622:d:10.1038_386279a0

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/386279a0

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().