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Galphao  -  G protein alpha o subunit

Drosophila melanogaster

Synonyms: Bkh, CG2204, DG[[o]], DGalpha0, DGalpha[[o]], ...
 
 
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Disease relevance of G-oalpha47A

  • Immunolocalization studies revealed that the Go alpha and Gs alpha homologs are expressed at highest levels in neuropils and at intermediate levels in the cortex of all brain and thoracic ganglion areas [1].
  • The alpha subunit of Go serves as a substrate for modification by pertussis toxin (PTX) [2].
 

High impact information on G-oalpha47A

  • Here, we show roles for the Galpha(o) subunit (Go) in mediating the two distinct pathways transduced by Fz receptors in Drosophila: the Wnt and planar polarity pathways [3].
  • The gene encoding the alpha subunit of the Drosophila Go protein is expressed early in embryogenesis in the precursor cells of the heart tube, of the visceral muscles, and of the nervous system [4].
  • In particular, the heart does not form properly and interruptions in the heart epithelium are repeatedly observed, henceforth the brokenheart (bkh) name [4].
  • In contrast to the wide distribution of Go alpha and Gs alpha, Gi alpha has a surprisingly restricted distribution in the CNS [1].
  • Western blot analysis of membranes prepared from Drosophila heads indicates that antibodies specific for the Drosophila Go alpha and Gs alpha homologs recognize the appropriate protein species predicted by molecular cloning (Quan et al., 1989; Thambi et al., 1989) [1].
 

Biological context of G-oalpha47A

 

Anatomical context of G-oalpha47A

 

Physical interactions of G-oalpha47A

  • Thus, Go is likely part of a trimeric G protein complex that directly transduces Fz signals from the membrane to downstream components [3].
 

Other interactions of G-oalpha47A

  • This set includes Galpha15, Galpha16, Galphaq, and chimeric Galphaq proteins with the last few amino acids of either Galphai2 (Galphaqi), Galphao (Galphaqo), or Galphaz (Galphaqz) [9].
 

Analytical, diagnostic and therapeutic context of G-oalpha47A

  • In situ hybridization of specific probes to tissue sections indicates that the mRNAs coding for Go alpha-like proteins in Drosophila are expressed primarily in neuronal cell bodies and, at lower levels, in the eyes [2].

References

  1. Immunolocalization of G protein alpha-subunits in the Drosophila CNS. Wolfgang, W.J., Quan, F., Goldsmith, P., Unson, C., Spiegel, A., Forte, M. J. Neurosci. (1990) [Pubmed]
  2. Immunological and molecular characterization of Go alpha-like proteins in the Drosophila central nervous system. Thambi, N.C., Quan, F., Wolfgang, W.J., Spiegel, A., Forte, M. J. Biol. Chem. (1989) [Pubmed]
  3. Trimeric G protein-dependent frizzled signaling in Drosophila. Katanaev, V.L., Ponzielli, R., Sémériva, M., Tomlinson, A. Cell (2005) [Pubmed]
  4. The heterotrimeric protein Go is required for the formation of heart epithelium in Drosophila. Frémion, F., Astier, M., Zaffran, S., Guillèn, A., Homburger, V., Sémériva, M. J. Cell Biol. (1999) [Pubmed]
  5. Molecular characterization of Drosophila gene encoding G0 alpha subunit homolog. Yoon, J., Shortridge, R.D., Bloomquist, B.T., Schneuwly, S., Perdew, M.H., Pak, W.L. J. Biol. Chem. (1989) [Pubmed]
  6. Neuronal expression of a newly identified Drosophila melanogaster G protein alpha 0 subunit. Schmidt, C.J., Garen-Fazio, S., Chow, Y.K., Neer, E.J. Cell Regul. (1989) [Pubmed]
  7. A Drosophila phospholipase C gene that is expressed in the central nervous system. Shortridge, R.D., Yoon, J., Lending, C.R., Bloomquist, B.T., Perdew, M.H., Pak, W.L. J. Biol. Chem. (1991) [Pubmed]
  8. Pertussis toxin expression in Drosophila alters the visual response and blocks eating behaviour. Fitch, C.L., de Sousa, S.M., O'Day, P.M., Neubert, T.A., Plantilla, C.M., Spencer, M., Yarfitz, S., Apte, D., Hurley, J.B. Cell. Signal. (1993) [Pubmed]
  9. The G protein-coupling profile of metabotropic glutamate receptors, as determined with exogenous G proteins, is independent of their ligand recognition domain. Parmentier, M.L., Joly, C., Restituito, S., Bockaert, J., Grau, Y., Pin, J.P. Mol. Pharmacol. (1998) [Pubmed]
 
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