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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Identification of ethanol responsive domains of adenylyl cyclase.

Background: The activity of adenylyl cyclase (AC) is enhanced by pharmacologically relevant concentrations of ethanol. The enhancing effect of ethanol on AC activity is AC isoform-specific. Therefore, we hypothesized that within a cyclic AMP-generating system, AC is the target of ethanol's action and that ethanol-sensitive AC molecules contain structural elements modulated by ethanol. The structural elements are designated as "ethanol responsive domains." Methods: By using a series of chimeric mutants, we searched regions of the AC molecule that are important for the ethanol effect. These chimeric mutants were derived from 3 isoforms of AC: AC7 (type 7), the most ethanol responsive isoform; AC3 (type 3), an isoform that is far less responsive to ethanol; and AC2 (type 2), an isoform that is homologous to AC7 but less responsive to ethanol. Results: We identified 2 discrete regions of the AC molecule that are important for the enhancement of AC activity by ethanol. The first is the N-terminal 28-amino-acid (aa) region of the C(1a) domain. The second is the C-terminal region ( approximately 140 aa) of the AC molecule. Sequence differences in the N-terminal tail, 2 putative transmembrane domains, and the C(1b) domain are not important for ethanol's effect. Conclusions: The current study with mammalian ACs provides a new class of alcohol-responsive protein and possibly a new mechanism of alcohol action on cellular function. The identification of ethanol responsive domains will facilitate the elucidation of the mechanisms by which ethanol enhances the activity of AC.[1]


  1. Identification of ethanol responsive domains of adenylyl cyclase. Yoshimura, M., Pearson, S., Kadota, Y., Gonzalez, C.E. Alcohol. Clin. Exp. Res. (2006) [Pubmed]
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