Delta glutamate receptors are functional glycine- and ᴅ-serine–gated cation channels in situ-Reference-Cited by-同舟云学术

Delta glutamate receptors are functional glycine- and ᴅ-serine–gated cation channels in situ

Published:2021-12-24 Issue:52 Volume:7 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Carrillo Elisa¹^ORCID,Gonzalez Cuauhtemoc U.¹²^ORCID,Berka Vladimir¹^ORCID,Jayaraman Vasanthi¹²^ORCID

Affiliation:

1. Center for Membrane Biology, Department of Biochemistry and Molecular Biology, University of Texas Health Science Center at Houston, 6431 Fannin St., Houston, TX 77030, USA.

2. MD Anderson Cancer Center UTHealth Graduate School of Biomedical Sciences, University of Texas Health Science Center at Houston, 6431 Fannin St., Houston, TX 77030, USA.

Abstract

The synaptic proteins cerebellin-1 and neurexin-1β permit ion channel activity in delta subtype of ionotropic glutamate receptors.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference43 articles.

1. Glutamate Receptor Ion Channels: Structure, Regulation, and Function

2. NMDA receptors: linking physiological output to biophysical operation

3. To Gate or not to Gate: Are the Delta Subunits in the Glutamate Receptor Family Functional Ion Channels?

4. Structural basis for integration of GluD receptors within synaptic organizer complexes

5. Conformational Plasticity in the Transsynaptic Neurexin-Cerebellin-Glutamate Receptor Adhesion Complex

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