| First Author | Brooks C | Year | 2018 |
| Journal | Front Mol Neurosci | Volume | 11 |
| Pages | 16 | PubMed ID | 29410614 |
| Mgi Jnum | J:281930 | Mgi Id | MGI:6380938 |
| Doi | 10.3389/fnmol.2018.00016 | Citation | Brooks C, et al. (2018) Farnesylation of the Transducin G Protein Gamma Subunit Is a Prerequisite for Its Ciliary Targeting in Rod Photoreceptors. Front Mol Neurosci 11:16 |
| abstractText | Primary cilia are microtubule-based organelles, which protrude from the plasma membrane and receive a wide range of extracellular signals. Various cilia use G protein-coupled receptors (GPCRs) for the detection of these signals. For instance, vertebrate rod photoreceptors use their cilia (also called outer segments) as antennae detecting photons by GPCR rhodopsin. Rhodopsin recognizes incoming light and activates its G protein, transducin, which is composed of three subunits alpha, beta, and gamma. Similar to all G protein gamma subunits, the transducin Ggamma1 subunit undergoes C-terminal prenylation resulting in the addition of an isoprenoid farnesyl; however, the significance of this posttranslational modification is unclear. To study the role of the farnesyl group, we genetically introduced a mutant Ggamma1 that lacked the prenylation site into the retinal photoreceptors of mice. The biochemical and physiological analyses of these mice revealed that mutant Ggamma1 dimerizes with the endogenous transducin Gbeta1 subunit and that the resulting Gbetagamma dimers display reduced hydrophobicity. Although mutant Gbetagamma dimers could form a heterotrimeric G protein, they could not mediate phototransduction. This deficiency was due to a strong exclusion of non-farnesylated Gbetagamma complexes from the cilia (rod outer segments). Our results provide the first evidence that farnesylation is required for trafficking of G-protein betagamma subunits to the cilium of rod photoreceptors. |
