A Cys-loop mutation in the Caenorhabditis elegans nicotinic receptor subunit UNC-63 impairs but does not abolish channel function.

Journal article

The nematode Caenorhabditis elegans is an established model organism for studying neurobiology. UNC-63 is a C. elegans nicotinic acetylcholine receptor (nAChR) α-subunit. It is an essential component of the levamisole-sensitive muscle nAChR (L-nAChR) and therefore plays an important role in cholinergic transmission at the nematode neuromuscular junction. Here, we show that worms with the unc-63(x26) allele, with its αC151Y mutation disrupting the Cys-loop, have deficient muscle function refle...

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Authors: Jones, A; Rayes, D; Al-Diwani, A; Maynard, T; Jones, R

• Publication status: Published
• Journal: Journal of biological chemistry
• Volume: 286
• Issue: 4
• Pages: 2550-2558
• Publication date: 2011-01-01
• DOI: 10.1074/jbc.m110.177238
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: 4-Aminopyridine; Animals; Potassium Channel Blockers; Caenorhabditis elegans; Neuromuscular Junction; Pyridostigmine Bromide; Cholinesterase Inhibitors; Myasthenic Syndromes, Congenital; Swimming; Mutation; Humans; Gene Expression Regulation; Caenorhabditis elegans Proteins; Muscles; Protein Structure, Secondary; Receptors, Nicotinic; Disease Models, Animal