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Gene Review

RHOG  -  ras homolog family member G

Homo sapiens

Synonyms: ARHG, MGC125835, MGC125836, Rho-related GTP-binding protein RhoG, RhoG
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Disease relevance of RHOG

  • Significantly higher levels of Rho-C and Rho-G were seen in patients who died of breast cancer than in those who remained disease free [1].
  • In addition, we report that SopB stimulates cellular responses by activating SH3-containing guanine nucleotide exchange factor (SGEF), an exchange factor for RhoG, which we found plays a central role in the actin cytoskeleton remodeling stimulated by Salmonella [2].
  • We show here that induction of Shigella entry foci is controlled by the Cdc42, Rac and Rho GTPases, but not by RhoG [3].
  • The analysis revealed that the 52 kDa FK506 binding protein, Rho G-protein dissociation inhibitor (RhoGDI), and glyoxalase I are found to be uniquely overexpressed in invasive human ovarian cancer when compared to the LMP form of this cancer [4].

High impact information on RHOG

  • Kinectin is a key effector of RhoG microtubule-dependent cellular activity [5].
  • We have identified a novel role for RhoG in signaling the neutrophil respiratory burst stimulated by G protein-coupled receptor agonists [6].
  • By screening a cDNA library of a mouse macrophage cell line, we identified two small GTPase family members (RhoG and Rab5) that enhanced the engulfment of apoptotic cells [7].
  • Phagocytosis of apoptotic cells is regulated by a UNC-73/TRIO-MIG-2/RhoG signaling module and armadillo repeats of CED-12/ELMO [8].
  • RESULTS: Here, we define a conserved signaling module involving the small GTPase RhoG and its exchange factor TRIO, which functions upstream of ELMO/Dock180/Rac during engulfment [8].

Biological context of RHOG

  • Hence, these results implicate RhoG in leukocyte trafficking and the control of gene expression induced in response to antigen encounter [9].
  • Here we investigated the role of RhoG in cell migration [10].
  • DNA array analysis revealed that expression of genes such as the RhoG and D4-GDI genes was down-regulated in TEL-overexpressing cells, while that of the representative growth-related genes such as the c-myc, c-fos and c-jun genes was not remarkably changed [11].

Anatomical context of RHOG

  • RhoG, kinectin, and kinesin colocalize in REF-52 and COS-7 cells, mainly in the endoplasmic reticulum but also in lysosomes [5].
  • Finally, transient transduction of a tat-tagged Rac1(17N) dominant-negative fusion protein inhibited the induction of lamellipodia by the Rac-specific activator, Tiam1, but not by activated RhoG [12].
  • RhoG, a member of the Rho family of GTPases, has been implicated as a regulator of the actin cytoskeleton [9].
  • In this study, we show a novel function for the small GTPase RhoG on the regulation of the interferon-gamma promoter and nuclear factor of activated T cells (NFAT) gene transcription in lymphocytes [9].
  • RhoG, a member related to Rac and Cdc42Hs, is activated at the transcriptional level in the mid-G1 phase of stimulated fibroblasts [13].

Associations of RHOG with chemical compounds

  • The RhoG-Elmo-Dock180 pathway is required for activation of Rac1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor [14].
  • The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids [15].
  • Our data suggest a role for the phosphoinositide 3-kinase, PI 3-kinase, in modulating the Trio/RhoG signaling pathway [15].
  • The PGE(2) level of irradiated cells was higher than in controls (1512 +/- 157.5 vs. 973.7 +/- 54.2 rhog PGE(2)/mL; p < 0.005, n = 4) while cells irradiated in the presence of NS-398 had reduced PGE(2) levels (218.8 +/- 80.1 rhog PGE(2)/mL; p < 0.005; n = 4) [16].
  • Steady-state PK of octreotide 20 mg/28 d suggested a C(mean) of 1216 rhog/mL (range, 1065-1585) with low fluctuation index (43%) [17].

Regulatory relationships of RHOG


Other interactions of RHOG

  • RhoGDI-3 is a new GDP dissociation inhibitor (GDI). Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG [20].
  • SGEF, a RhoG guanine nucleotide exchange factor that stimulates macropinocytosis [18].
  • Scanning electron microscopy of fibroblasts demonstrated that SGEF induced dorsal ruffles that were morphologically similar to those generated by constitutively active RhoG, but not constitutively active Rac1 [18].
  • Node-positive tumors have significantly higher levels of Rho-C and Rho-G, and lower levels of Rho-GDI and Rho-GDI-gamma transcripts, than do node-negative tumors [1].
  • Trio contains two DH/PH tandem domains that respectively activate the small GTPases RhoG/Rac and RhoA [21].

Analytical, diagnostic and therapeutic context of RHOG


  1. Prognostic value of rho GTPases and rho guanine nucleotide dissociation inhibitors in human breast cancers. Jiang, W.G., Watkins, G., Lane, J., Cunnick, G.H., Douglas-Jones, A., Mokbel, K., Mansel, R.E. Clin. Cancer Res. (2003) [Pubmed]
  2. Differential activation and function of Rho GTPases during Salmonella-host cell interactions. Patel, J.C., Gal??n, J.E. J. Cell Biol. (2006) [Pubmed]
  3. Rho family GTPases control entry of Shigella flexneri into epithelial cells but not intracellular motility. Mounier, J., Laurent, V., Hall, A., Fort, P., Carlier, M.F., Sansonetti, P.J., Egile, C. J. Cell. Sci. (1999) [Pubmed]
  4. Proteomic analysis and identification of new biomarkers and therapeutic targets for invasive ovarian cancer. Jones, M.B., Krutzsch, H., Shu, H., Zhao, Y., Liotta, L.A., Kohn, E.C., Petricoin, E.F. Proteomics (2002) [Pubmed]
  5. Kinectin is a key effector of RhoG microtubule-dependent cellular activity. Vignal, E., Blangy, A., Martin, M., Gauthier-Rouvière, C., Fort, P. Mol. Cell. Biol. (2001) [Pubmed]
  6. RhoG Regulates the Neutrophil NADPH Oxidase. Condliffe, A.M., Webb, L.M., Ferguson, G.J., Davidson, K., Turner, M., Vigorito, E., Manifava, M., Chilvers, E.R., Stephens, L.R., Hawkins, P.T. J. Immunol. (2006) [Pubmed]
  7. Opposite effects of rho family GTPases on engulfment of apoptotic cells by macrophages. Nakaya, M., Tanaka, M., Okabe, Y., Hanayama, R., Nagata, S. J. Biol. Chem. (2006) [Pubmed]
  8. Phagocytosis of apoptotic cells is regulated by a UNC-73/TRIO-MIG-2/RhoG signaling module and armadillo repeats of CED-12/ELMO. deBakker, C.D., Haney, L.B., Kinchen, J.M., Grimsley, C., Lu, M., Klingele, D., Hsu, P.K., Chou, B.K., Cheng, L.C., Blangy, A., Sondek, J., Hengartner, M.O., Wu, Y.C., Ravichandran, K.S. Curr. Biol. (2004) [Pubmed]
  9. RhoG regulates gene expression and the actin cytoskeleton in lymphocytes. Vigorito, E., Billadeu, D.D., Savoy, D., McAdam, S., Doody, G., Fort, P., Turner, M. Oncogene (2003) [Pubmed]
  10. Activation of Rac1 by RhoG regulates cell migration. Katoh, H., Hiramoto, K., Negishi, M. J. Cell. Sci. (2006) [Pubmed]
  11. Effects of overexpression of the Ets family transcription factor TEL on cell growth and differentiation of K562 cells. Sakurai, T., Yamada, T., Kihara-Negishi, F., Teramoto, S., Sato, Y., Izawa, T., Oikawa, T. Int. J. Oncol. (2003) [Pubmed]
  12. RhoG signals in parallel with Rac1 and Cdc42. Wennerberg, K., Ellerbroek, S.M., Liu, R.Y., Karnoub, A.E., Burridge, K., Der, C.J. J. Biol. Chem. (2002) [Pubmed]
  13. Structure of the human ARHG locus encoding the Rho/Rac-like RhoG GTPase. Le Gallic, L., Fort, P. Genomics (1997) [Pubmed]
  14. RhoG activates Rac1 by direct interaction with the Dock180-binding protein Elmo. Katoh, H., Negishi, M. Nature (2003) [Pubmed]
  15. The C-terminal basic tail of RhoG assists the guanine nucleotide exchange factor trio in binding to phospholipids. Skowronek, K.R., Guo, F., Zheng, Y., Nassar, N. J. Biol. Chem. (2004) [Pubmed]
  16. Radiation induces upregulation of cyclooxygenase-2 (COX-2) protein in PC-3 cells. Steinauer, K.K., Gibbs, I., Ning, S., French, J.N., Armstrong, J., Knox, S.J. Int. J. Radiat. Oncol. Biol. Phys. (2000) [Pubmed]
  17. Long-acting octreotide and prolonged-release lanreotide formulations have different pharmacokinetic profiles. Astruc, B., Marbach, P., Bouterfa, H., Denot, C., Safari, M., Vitaliti, A., Sheppard, M. Journal of clinical pharmacology. (2005) [Pubmed]
  18. SGEF, a RhoG guanine nucleotide exchange factor that stimulates macropinocytosis. Ellerbroek, S.M., Wennerberg, K., Arthur, W.T., Dunty, J.M., Bowman, D.R., DeMali, K.A., Der, C., Burridge, K. Mol. Biol. Cell (2004) [Pubmed]
  19. Dock4 is regulated by RhoG and promotes Rac-dependent cell migration. Hiramoto, K., Negishi, M., Katoh, H. Exp. Cell Res. (2006) [Pubmed]
  20. RhoGDI-3 is a new GDP dissociation inhibitor (GDI). Identification of a non-cytosolic GDI protein interacting with the small GTP-binding proteins RhoB and RhoG. Zalcman, G., Closson, V., Camonis, J., Honoré, N., Rousseau-Merck, M.F., Tavitian, A., Olofsson, B. J. Biol. Chem. (1996) [Pubmed]
  21. Crystallization and initial crystal characterization of the N-terminal DH/PH domain of Trio. Skowronek, K., Ghumman, M., Zheng, Y., Nassar, N. Acta Crystallogr. D Biol. Crystallogr. (2003) [Pubmed]
  22. Localization of ARHG, a member of the RAS homolog gene family, to 11p15.5-11p15.4 by fluorescence in situ hybridization. Taviaux, S.A., Vincent, S., Fort, P., Demaille, J.G. Genomics (1993) [Pubmed]
  23. The effects of propofol on lipid peroxidation and inflammatory response in elective coronary artery bypass grafting. Corcoran, T.B., Engel, A., Sakamoto, H., O'Callaghan-Enright, S., O'Donnell, A., Heffron, J.A., Shorten, G. J. Cardiothorac. Vasc. Anesth. (2004) [Pubmed]
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