Looking below the surface of nicotinic acetylcholine receptors

Clare Stokes, Millet Treinin, Roger L. Papke*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

74 Scopus citations

Abstract

The amino acid sequences of nicotinic acetylcholine receptors (nAChRs) from diverse species can be compared across extracellular, transmembrane, and intracellular domains. The intracellular domains are most divergent among subtypes, yet relatively consistent among species. The diversity indicates that each nAChR subtype has a unique language for communication with its host cell. The conservation across species also suggests that the intracellular domains have defining functional roles for each subtype. Secondary structure prediction indicates two relatively conserved alpha helices within the intracellular domains of all nAChRs. Among all subtypes, the intracellular domain of α7 nAChR is one of the most well conserved, and α7 nAChRs have effects in non-neuronal cells independent of generating ion currents, making it likely that the α7 intracellular domain directly mediates signal transduction. There are potential phosphorylation and protein-binding sites in the α7 intracellular domain, which are conserved and may be the basis for α7-mediated signal transduction.

Original languageAmerican English
Article number1237
Pages (from-to)514-523
Number of pages10
JournalTrends in Pharmacological Sciences
Volume36
Issue number8
DOIs
StatePublished - 11 Aug 2015

Bibliographical note

Funding Information:
The authors thank Nicole Horenstein, Dietlind Gerloff, and Eliot Spindel for comments and suggestions. This work was supported by National Institute of Health grant RO1-GM57481.

Publisher Copyright:
© 2015 Elsevier Ltd.

Keywords

  • cys-loop receptors
  • evolution
  • intracellular domains
  • protein structure
  • proteomics
  • signal transduction

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