G-iα65A, Gαi, G-ialpha65A, Giα, Gi
G protein α subunit involved in regulating asymmetric cell division - Ric-8 regulates Gαi cortical localization to promote Gαi-dependent planar orientation of the mitotic spindle during asymmetric cell division
Gene model reviewed during 5.40
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.50
There is only one protein coding transcript and one polypeptide associated with this gene
G proteins are composed of 3 units; alpha, beta and gamma. The alpha chain contains the guanine nucleotide binding site. Interacts (via GDP- or GTP-bound forms) with loco (via GoLoco and RGS domains). Interacts with raps/pins.
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Gαi using the Feature Mapper tool.
G-oα65A protein staining appears at stage S10B of oogenesis, in a few granules in the oocyte, and in dorsal anterior follicle cells. By stage S12, more protein is detected in the oocytes, and all follicle cells stain. The oocyte contains high levels of uniformly distributed granules at the end of oogenesis. The distribution of G-oα65A protein is uniform in embryonic cleavage stages 1-2, becomes restricted to the posterior pole by cleavage stage 4, and has disappeared by the end of the blastoderm stage. The protein reappears at stage 14 in presumptive cardioblast cells, and this staining persists into larval stages. After stage 15, chordotonal organ and ring gland precursors express G-oα65A protein. Staining is also detected in a subset of cell bodies in the ventral ganglion, and in additional CNS cells.
Low levels of G-oα65A protein are detected throughout the CNS in both the cortex and neuropil. Higher levels of expression are detected at the terminations of photoreceptor cells in the lamina and medulla. Some staining is also detected in the ocellar retina and the antennal glomerulae, as well as in the proximal half of the ocellar nerve. Some expression is detected in the retina.
GBrowse - Visual display of RNA-Seq signalsView Dmel\Gαi in GBrowse 2
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
dsRNA made from templates generated with primers directed against this gene tested in RNAi screen for effects on Kc167 and S2R+ cell morphology.
Overexpression of G-iα65A results in defects in both spindle orientation and determinant localisation in neuroblasts and sensory organ precursor cells.
Dominant adult phenotypes can be caused by the overexpression of activated Gα proteins.
Posterior localization of the G-iα65A protein during early embryogenesis requires a subset of the posterior group genes.
G-iα65A protein expression in the adult Drosophila central nervous system has been studied.
Isolated from a genomic library using bovine rod and cone transducin α subunit cDNAs as probe.
G proteins belong to a family of membrane-associated guanine nucleotide-binding proteins that couple specific receptors for extracellular signals to specific intracellular effectors, thus regulating the activity of these effectors. When not interacting with the receptor, G proteins are usually in the form of a heterotrimer made up of α, β and γ subunits, with the α subunit bound to GDP. Upon activation by the receptor, the α subunit exchanges GDP for GTP, dissociates from the β-γ subunits and interacts with the effector. Afterwards GTP is hydrolyzed and the heterotrimer of α, β and γ subunits is formed again.
Encodes a G protein α subunit displaying sequence homology to mammalian Giα that inhibits adenylate cyclase activity. The G protein is uniformly distributed in oocytes, becomes restricted to the posterior pole of the embryo during early cleavage and is lost during the blastoderm stage (Wolfgang et al., 1990).