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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Lazar, Josef Bondar, Alexey |
| Description | Author Affiliation: Bondar A ( From the Faculty of Science, University of South Bohemia, Branisovska 31a, 37005 Ceske Budejovice, Czech Republic and.) |
| Abstract | Although most heterotrimeric G proteins are thought to dissociate into G and Gßγ subunits upon activation, the evidence in the Gi/o family has long been inconsistent and contradictory. The Gi/o protein family mediates inhibition of cAMP production and regulates the activity of ion channels. On the basis of experimental evidence, both heterotrimer dissociation and rearrangement have been postulated as crucial steps of Gi/o protein activation and signal transduction. We have now investigated the process of Gi/o activation in living cells directly by two-photon polarization microscopy and indirectly by observations of G protein-coupled receptor kinase-derived polypeptides. Our observations of existing fluorescently labeled and non-modified G i/o constructs indicate that the molecular mechanism of G i/o activation is affected by the presence and localization of the fluorescent label. All investigated non-labeled, non-modified Gi/o complexes dissociate extensively upon activation. The dissociated subunits can activate downstream effectors and are thus likely to be the major activated Gi/o form. Constructs of G i/o subunits fluorescently labeled at the N terminus (GAP43-CFP-G i/o) seem to faithfully reproduce the behavior of the non-modified G i/o subunits. G i constructs labeled within the helical domain (G i-L91-YFP) largely do not dissociate upon activation, yet still activate downstream effectors, suggesting that the dissociation seen in non-modified G i/o proteins is not required for downstream signaling. Our results appear to reconcile disparate published data and settle a long running dispute. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 3 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-01-17 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | GAP-43 Protein Metabolism GTP-Binding Protein Alpha Subunits, Gi-Go GTP-Binding Protein Beta Subunits GTP-Binding Protein Gamma Subunits Enzyme Activation Physiology Genetics HEK293 Cells Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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