Three functional isoforms of GAR-2, a Caenorhabditis elegans G-protein-linked acetylcholine receptor, are produced by alternative splicing

Su Jeong Suh, Yang Seo Park, Yong-Seok Lee, Tae Ju Cho, Bong Kiun Kaang, Nam Jeong Cho

Research output: Contribution to journalArticleResearchpeer-review

4 Citations (Scopus)

Abstract

We have previously isolated a cDNA clone from Caenorhabditis elegans that encodes a novel form of G-protein-linked acetylcholine receptor, termed GAR-2. GAR-2 is similar to but pharmacologically distinct from muscarinic acetylcholine receptors. Here we report the identification of two gar-2 cDNA clones that are different from the previous one. These newly identified cDNAs encode polypeptides of 664 and 627 amino acids, whereas the previous one encodes a polypeptide of 614 amino acids. The three GAR-2 isoforms, which differ only in the third intracellular loop, arise from alternative splicing. Electrophysiological analyses using the Xenopus oocyte system showed that all three GAR-2 isoforms couple to the activation of G-protein-gated inwardly rectifying K+ (GIRK1) channel with similar drug specificity. Our results indicate that alternative splicing plays an important role in promoting molecular diversity of G-protein-linked acetylcholine receptors in C. elegans.

Original languageEnglish
Pages (from-to)1238-1243
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume288
Issue number5
DOIs
StatePublished - 16 Nov 2001

Fingerprint

Caenorhabditis elegans Proteins
Alternative Splicing
Cholinergic Receptors
GTP-Binding Proteins
Protein Isoforms
Complementary DNA
Caenorhabditis elegans
Clone Cells
Inwardly Rectifying Potassium Channel
Amino Acids
Peptides
Muscarinic Receptors
Xenopus
Oocytes
Chemical activation
Pharmaceutical Preparations

Keywords

  • Alternative splicing
  • Caenorhabditis elegans
  • G-protein-linked acetylcholine receptor
  • Gar-2

Cite this

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title = "Three functional isoforms of GAR-2, a Caenorhabditis elegans G-protein-linked acetylcholine receptor, are produced by alternative splicing",
abstract = "We have previously isolated a cDNA clone from Caenorhabditis elegans that encodes a novel form of G-protein-linked acetylcholine receptor, termed GAR-2. GAR-2 is similar to but pharmacologically distinct from muscarinic acetylcholine receptors. Here we report the identification of two gar-2 cDNA clones that are different from the previous one. These newly identified cDNAs encode polypeptides of 664 and 627 amino acids, whereas the previous one encodes a polypeptide of 614 amino acids. The three GAR-2 isoforms, which differ only in the third intracellular loop, arise from alternative splicing. Electrophysiological analyses using the Xenopus oocyte system showed that all three GAR-2 isoforms couple to the activation of G-protein-gated inwardly rectifying K+ (GIRK1) channel with similar drug specificity. Our results indicate that alternative splicing plays an important role in promoting molecular diversity of G-protein-linked acetylcholine receptors in C. elegans.",
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Three functional isoforms of GAR-2, a Caenorhabditis elegans G-protein-linked acetylcholine receptor, are produced by alternative splicing. / Suh, Su Jeong; Park, Yang Seo; Lee, Yong-Seok; Cho, Tae Ju; Kaang, Bong Kiun; Cho, Nam Jeong.

In: Biochemical and Biophysical Research Communications, Vol. 288, No. 5, 16.11.2001, p. 1238-1243.

Research output: Contribution to journalArticleResearchpeer-review

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