Modelling the consequences of receptor-G-protein promiscuity
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
PubMed
11931992
DOI
10.1016/s0165-6147(00)01996-9
PII: S0165-6147(00)01996-9
Knihovny.cz E-resources
- MeSH
- Adenylyl Cyclases metabolism physiology MeSH
- Models, Biological * MeSH
- Humans MeSH
- GTP-Binding Protein alpha Subunits, Gi-Go metabolism physiology MeSH
- GTP-Binding Protein alpha Subunits, Gs metabolism physiology MeSH
- GTP-Binding Proteins metabolism physiology MeSH
- Receptors, Cell Surface metabolism physiology MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- Adenylyl Cyclases MeSH
- GTP-Binding Protein alpha Subunits, Gi-Go MeSH
- GTP-Binding Protein alpha Subunits, Gs MeSH
- GTP-Binding Proteins MeSH
- Receptors, Cell Surface MeSH
Many G-protein-coupled receptors interact with more than one type of G protein, giving rise to extreme variability in the effects of receptor activation, depending on, for example, receptor density and desensitization, efficacy of agonists, and availability of specific G proteins. This leads to errors in interpretation of data. To facilitate understanding the consequences of receptor-G-protein promiscuity, we use two simplified models to simulate such consequences. Applied to the regulation of adenylyl cyclase and phosphoinositidase, the models predict seemingly paradoxical situations and explain some phenomena that, at first sight, might seem to require the induction of agonist-specific (G-protein-selective) receptor conformations.
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