Alternative splicing generates two isoforms of the α2 subunit of the inhibitory glycine receptor

J. Kuhse, A. Kuryatov, Y. Maulet, M. L. Malosio, V. Schmieden, H. Betz

Research output: Contribution to journalArticle

Abstract

The inhibitory glycine receptor (GlyR) is a ligand-gated chloride channel protein which displays developmental heterogeneity in the mammalian central nervous system. Here we describe 2 novel cDNA variants of the rat GlyR α2 subunit and demonstrate that alternative splicing generates these 2 isoforms. The deduced protein sequences (α2A and α2B) exhibit 99% identity with the previously characterized human α2 subunit. In situ hybridization revealed expression of both α2A und α2B mRNAs in the prenatal rat brain, suggesting that these variant proteins may have a role in synaptogenesis. Heterologous expression in Xenopus oocytes showed that the more abundantly expressed α2A subunit forms strychnine-sensitive ion channels which resemble human α2 subunit GlyRs in their electrophysiological properties.

Original languageEnglish
Pages (from-to)73-77
Number of pages5
JournalFEBS Letters
Volume283
Issue number1
DOIs
Publication statusPublished - May 20 1991

Fingerprint

Glycine Receptors
Alternative Splicing
Protein Isoforms
Rats
Ligand-Gated Ion Channels
Strychnine
Chloride Channels
Proteins
Neurology
Xenopus
Ion Channels
Oocytes
In Situ Hybridization
Brain
Central Nervous System
Complementary DNA
Ligands
Messenger RNA

Keywords

  • Alternative splicing
  • Brain development
  • Glycine receptor
  • Receptor heterogeneity

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology
  • Cell Biology
  • Genetics
  • Structural Biology

Cite this

Alternative splicing generates two isoforms of the α2 subunit of the inhibitory glycine receptor. / Kuhse, J.; Kuryatov, A.; Maulet, Y.; Malosio, M. L.; Schmieden, V.; Betz, H.

In: FEBS Letters, Vol. 283, No. 1, 20.05.1991, p. 73-77.

Research output: Contribution to journalArticle

Kuhse, J. ; Kuryatov, A. ; Maulet, Y. ; Malosio, M. L. ; Schmieden, V. ; Betz, H. / Alternative splicing generates two isoforms of the α2 subunit of the inhibitory glycine receptor. In: FEBS Letters. 1991 ; Vol. 283, No. 1. pp. 73-77.
@article{a681c15e13ef468a9b3b250ae661c640,
title = "Alternative splicing generates two isoforms of the α2 subunit of the inhibitory glycine receptor",
abstract = "The inhibitory glycine receptor (GlyR) is a ligand-gated chloride channel protein which displays developmental heterogeneity in the mammalian central nervous system. Here we describe 2 novel cDNA variants of the rat GlyR α2 subunit and demonstrate that alternative splicing generates these 2 isoforms. The deduced protein sequences (α2A and α2B) exhibit 99{\%} identity with the previously characterized human α2 subunit. In situ hybridization revealed expression of both α2A und α2B mRNAs in the prenatal rat brain, suggesting that these variant proteins may have a role in synaptogenesis. Heterologous expression in Xenopus oocytes showed that the more abundantly expressed α2A subunit forms strychnine-sensitive ion channels which resemble human α2 subunit GlyRs in their electrophysiological properties.",
keywords = "Alternative splicing, Brain development, Glycine receptor, Receptor heterogeneity",
author = "J. Kuhse and A. Kuryatov and Y. Maulet and Malosio, {M. L.} and V. Schmieden and H. Betz",
year = "1991",
month = "5",
day = "20",
doi = "10.1016/0014-5793(91)80557-J",
language = "English",
volume = "283",
pages = "73--77",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Alternative splicing generates two isoforms of the α2 subunit of the inhibitory glycine receptor

AU - Kuhse, J.

AU - Kuryatov, A.

AU - Maulet, Y.

AU - Malosio, M. L.

AU - Schmieden, V.

AU - Betz, H.

PY - 1991/5/20

Y1 - 1991/5/20

N2 - The inhibitory glycine receptor (GlyR) is a ligand-gated chloride channel protein which displays developmental heterogeneity in the mammalian central nervous system. Here we describe 2 novel cDNA variants of the rat GlyR α2 subunit and demonstrate that alternative splicing generates these 2 isoforms. The deduced protein sequences (α2A and α2B) exhibit 99% identity with the previously characterized human α2 subunit. In situ hybridization revealed expression of both α2A und α2B mRNAs in the prenatal rat brain, suggesting that these variant proteins may have a role in synaptogenesis. Heterologous expression in Xenopus oocytes showed that the more abundantly expressed α2A subunit forms strychnine-sensitive ion channels which resemble human α2 subunit GlyRs in their electrophysiological properties.

AB - The inhibitory glycine receptor (GlyR) is a ligand-gated chloride channel protein which displays developmental heterogeneity in the mammalian central nervous system. Here we describe 2 novel cDNA variants of the rat GlyR α2 subunit and demonstrate that alternative splicing generates these 2 isoforms. The deduced protein sequences (α2A and α2B) exhibit 99% identity with the previously characterized human α2 subunit. In situ hybridization revealed expression of both α2A und α2B mRNAs in the prenatal rat brain, suggesting that these variant proteins may have a role in synaptogenesis. Heterologous expression in Xenopus oocytes showed that the more abundantly expressed α2A subunit forms strychnine-sensitive ion channels which resemble human α2 subunit GlyRs in their electrophysiological properties.

KW - Alternative splicing

KW - Brain development

KW - Glycine receptor

KW - Receptor heterogeneity

UR - http://www.scopus.com/inward/record.url?scp=0025828317&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025828317&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(91)80557-J

DO - 10.1016/0014-5793(91)80557-J

M3 - Article

C2 - 1645300

AN - SCOPUS:0025828317

VL - 283

SP - 73

EP - 77

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 1

ER -