Heterotrimeric G-proteins and their role in opioid receptor function
Heterotrimeric G-proteins are signal transducers of heptahelical receptors. They consist of a and bg subunits, both capable of interacting with several different effectors. Specific domains in their structures enable them to connect different intracellular signaling cascades, such as the adenylyl cy...
Elmentve itt :
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| Dokumentumtípus: | Cikk |
| Megjelent: |
2001
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| Sorozat: | Acta biologica Szegediensis
45 No. 1-4 |
| Kulcsszavak: | Természettudomány, Biológia |
| Online Access: | http://acta.bibl.u-szeged.hu/22441 |
| Tartalmi kivonat: | Heterotrimeric G-proteins are signal transducers of heptahelical receptors. They consist of a and bg subunits, both capable of interacting with several different effectors. Specific domains in their structures enable them to connect different intracellular signaling cascades, such as the adenylyl cyclase, phosphoinositol-bisphosphate or MAP kinase pathways. Their activity is synchronized by several components, one of them being a new protein family termed RGS (regulators of G-protein signaling). Members of this family inhibit the G-protein function. The intracellular localization of G-proteins indicates their role in plasma membrane-independent processes. Opioid receptors transmit their signals mainly via Gi/o proteins. Although the heterogeneity of opioid ligands (peptides and alkaloids) and their receptors (m, d, k and suggested subtypes in these classes) reveals a complicated picture, their unique characteristic of a high dependence capacity can not be explained without the analysis of the G-protein function. |
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| Terjedelem/Fizikai jellemzők: | 13-21 |
| ISSN: | 1588-385X |