Endocytosis function of a ligand-gated ion channel homolog in Caenorhabditis elegans.
Curr Biol
; 15(11): 1045-50, 2005 Jun 07.
Article
en En
| MEDLINE
| ID: mdl-15936276
ABSTRACT
Ligand-gated ion channels are transmembrane proteins that respond to a variety of transmitters, including acetylcholine, gamma-aminobutyric acid (GABA), glycine, and glutamate [1 and 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 alpha7 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.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Receptores Nicotínicos
/
Caenorhabditis elegans
/
Proteínas de Caenorhabditis elegans
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Endocitosis
/
Canales Iónicos
Límite:
Animals
Idioma:
En
Revista:
Curr Biol
Asunto de la revista:
BIOLOGIA
Año:
2005
Tipo del documento:
Article
País de afiliación:
Estados Unidos