ArticleJournal of molecular neuroscience : MN2006
The C-terminal T peptide of cholinesterases: structure, interactions, and influence on protein folding and secretion.
Article in Journal of molecular neuroscience : MN, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Different cholinesterase inhibitor effects on CSF cholinesterases in Alzheimer patients.Current Alzheimer research · 2009Trial
- AChR β-Subunit mRNAs Are Stabilized by HuR in a Mouse Model of Congenital Myasthenic Syndrome With Acetylcholinesterase Deficiency.Frontiers in molecular neuroscience · 2020Article
- Naturally Occurring Genetic Variants of Human Acetylcholinesterase and Butyrylcholinesterase and Their Potential Impact on the Risk of Toxicity from Cholinesterase Inhibitors.Chemical research in toxicology · 2016Review
- Acetylcholinesterase conformational states influence nitric oxide mobilization in the erythrocyte.The Journal of membrane biology · 2015Article
- Reassessment of the role of the central cholinergic system.Journal of molecular neuroscience : MN · 2014Review
- Contributions of selective knockout studies to understanding cholinesterase disposition and function.Chemico-biological interactions · 2010Article
- Targeting acetylcholinesterase to membrane rafts: a function mediated by the proline-rich membrane anchor (PRiMA) in neurons.The Journal of biological chemistry · 2010Article
- Upregulation of alpha7 Nicotinic Receptors by Acetylcholinesterase C-Terminal Peptides.PloS one · 2009Article
- Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mammalian cholinergic tissues mostly express the T splice variant of acetylcholinesterase, in which the catalytic domain is associated with a C-terminal peptide of 40 residues, called the t peptide (Massoulié, 2002). Homologous t peptides exist in all vertebrate cholinesterases, acetylcholinesterases (AChEs), and butyrylcholinesterases (BChEs): they contain a series of seven conserved aromatic residues, including three tryptophans, and a cysteine at position-4 of their C-terminus. The major AChE isozyme of the nematode Caenorhabditis elegans also contains a similar peptide. Although the C-terminal t peptides do not seem to affect the catalytic activity of cholinesterases, they determine their physiological function, because they allow cholinesterase subunits of type T to form oligomers and to associate with structural anchoring proteins. When reduced to their catalytic domain, AChE subunits without a t peptide are active but remain monomeric and soluble.
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Registered trials
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