Endocytosis function of a ligand-gated ion channel homolog in Caenorhabditis elegans

Andrea Patton, Sarah Knuth, Basil Schaheen, Hope Dang, Iva Greenwald, Hanna Fares

Research output: Contribution to journalArticle

43 Scopus citations

Abstract

Ligand-gated ion channels are transmembrane proteins that respond to a variety of transmitters, including acetylcholine, γ-aminobutyric acid (GABA), glycine, and glutamate [1, 2]. These proteins play key roles in neurotransmission and are typically found in the nervous system and at neuromuscular junctions [3]. Recently, acetylcholine receptor family members also have been found in nonneuronal cells, including macrophages [4], keratinocytes [5], bronchial epithelial cells [5], and endothelial cells of arteries [6]. The function of these channels in nonneuronal cells in mammals remains to be elucidated, though it has been shown that the acetylcholine receptor α7 subunit is required for acetylcholine-mediated inhibition of tumor necrosis factor release by activated macrophages [4]. We show that cup-4, a gene required for efficient endocytosis of fluids by C. elegans coelomocytes, encodes a protein that is homologous to ligand-gated ion channels, with the highest degree of similarity to nicotinic acetylcholine receptors. Worms lacking CUP-4 have reduced phosphatidylinositol 4,5-bisphosphate levels at the plasma membrane, suggesting that CUP-4 regulates endocytosis through modulation of phospholipase C activity.

Original languageEnglish (US)
Pages (from-to)1045-1050
Number of pages6
JournalCurrent Biology
Volume15
Issue number11
DOIs
StatePublished - Jun 7 2005

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Agricultural and Biological Sciences(all)

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