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Gene Review

Rhob  -  ras homolog gene family, member B

Mus musculus

Synonyms: AA017882, Arh6, Arhb, Rho-related GTP-binding protein RhoB
 
 
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Disease relevance of Rhob

 

Psychiatry related information on Rhob

 

High impact information on Rhob

  • RhoB controls Akt trafficking and stage-specific survival of endothelial cells during vascular development [2].
  • Moreover, pharmaceutical means to deplete RhoB in neonatal rats is associated with apoptosis in the sprouting endothelial cells of newly forming vessels [2].
  • In this study, we demonstrate a novel and critical role for the small GTPase, RhoB, in vascular development [2].
  • Likewise, the Vav-2 oncoprotein synergizes with RhoA and RhoB proteins in cellular transformation [6].
  • Yeast two-hybrid screening and coimmunoprecipitation have revealed that the GTP-bound form of RhoB and components of the cytoskeleton are protein partners of rhophilin 2 [7].
 

Biological context of Rhob

  • Akt mediates Ras downregulation of RhoB, a suppressor of transformation, invasion, and metastasis [1].
  • RhoB is an endosomal small GTPase that is implicated in the response to growth factors, genotoxic stress, and farnesyltransferase inhibitors [8].
  • Loss of RhoB did not adversely affect mouse development, fertility, or wound healing [8].
  • RhoB is dispensable for mouse development, but it modifies susceptibility to tumor formation as well as cell adhesion and growth factor signaling in transformed cells [8].
  • We have first demonstrated here that RhoB expression inhibits radiation-induced mitotic cell death [9].
 

Anatomical context of Rhob

  • Similarly, acute depletion of RhoB by antisense or dominant-negative strategies in primary endothelial cell culture models led to apoptosis and failures in tube formation [2].
  • However, embryo fibroblasts cultured in vitro exhibited a defect in motility, suggesting that RhoB has a role in this process that is conditional on cell stress [8].
  • Mechanistic investigations indicated that RhoB mediated transcriptional suppression but also accumulation of Cyclin B1 in the cytosol at early times after FTI treatment, at a time before the subsequent reduction in steady-state protein levels [10].
  • Farnesylated RhoB inhibits radiation-induced mitotic cell death and controls radiation-induced centrosome overduplication [9].
  • LPA also induced translocation of CDC42Hs to the membranes but had no effect on the distribution of Rac1, RhoB, or Rho-GDI [11].
 

Associations of Rhob with chemical compounds

  • Elevated rhoB mRNA was accompanied by an increase in RhoB protein, as detected by C3-mediated [32P]ADP-ribosylation [12].
  • Our findings suggest that RhoB is a negative regulator of integrin and growth factor signals that are involved in neoplastic transformation and possibly other stress or disease states [8].
  • Simvastatin increased RhoB protein levels by 8- to 10-fold [13].
  • Isoprenylation of RhoB is necessary for its degradation. A novel determinant in the complex regulation of RhoB expression by the mevalonate pathway [13].
  • Cholesterol supplementation did not prevent simvastatin-elicited up-regulation but increased RhoB levels per se [13].
 

Physical interactions of Rhob

 

Regulatory relationships of Rhob

  • RhoA and Cdc42 expression were sequentially upregulated and peaked during the commitment period while that of RhoB was induced in post-mitotic neurons [4].
  • In keeping with this, Src controls the actin dependence of RhoB endosome movement toward the plasma membrane [15].
  • Knocking out RhoB or expressing a dominant-interfering Rab11 mutant suppresses both catalytic activation of Src and translocation of active kinase to peripheral membrane structures [15].
 

Other interactions of Rhob

  • RhoA and Cdc42 were mainly cytosolic and RhoB particulate in the P19 cell model [4].
  • Therefore, we propose a model in which UVL induces stress-activated signal transduction leading to nuclear/cytoplasmic shuttling of HuR and subsequent stabilization of RhoB mRNA [14].
  • RhoB and actin polymerization coordinate Src activation with endosome-mediated delivery to the membrane [15].
  • Among several small Rho GTPases observed in the chick retina, RhoB was transiently expressed during development and mainly present in glial Müller cells in the adult [3].
  • This study reveals the selective expression of RhoB in the lens during early eye development and suggests a potential role for this small GTPase in cytoskeletal reorganization associated with lens epithelial cell elongation and differentiation [16].
 

Analytical, diagnostic and therapeutic context of Rhob

  • Confocal microscopy revealed that RhoB is highly localized to the nuclear margin with a small percentage found inside the nucleus [2].
  • In vitro mobility shift assays demonstrated that HuR bound the 3'-UTR of RhoB at three distinct locations (nucleotides 1342-1696, 1765-1920 and 1897-1977) suggesting a regulatory role for this RNA-binding protein [14].
  • HuR immunoprecipitations were positive for RhoB mRNA indicating an in vivo association, and Western blot analysis and immunofluorescence demonstrated that HuR rapidly partitions from the nucleus to the cytoplasm after UVL [14].
  • Applying the recently developed DNA array technique to a murine stroke model, we found that the gene coding for RhoB, a member of the family of GTPases that regulate a variety of signal transduction pathways, is upregulated in ischemia-damaged neurons [17].

References

  1. Akt mediates Ras downregulation of RhoB, a suppressor of transformation, invasion, and metastasis. Jiang, K., Sun, J., Cheng, J., Djeu, J.Y., Wei, S., Sebti, S. Mol. Cell. Biol. (2004) [Pubmed]
  2. RhoB controls Akt trafficking and stage-specific survival of endothelial cells during vascular development. Adini, I., Rabinovitz, I., Sun, J.F., Prendergast, G.C., Benjamin, L.E. Genes Dev. (2003) [Pubmed]
  3. Small GTP-binding protein RhoB is expressed in glial Müller cells in the vertebrate retina. Santos-Bredariol, A.S., Belmonte, M.A., Kihara, A.H., Santos, M.F., Hamassaki, D.E. J. Comp. Neurol. (2006) [Pubmed]
  4. RhoB expression is induced after the transient upregulation of RhoA and Cdc42 during neuronal differentiation and influenced by culture substratum and microtubule integrity. Laplante, I., Paquin, J., Béliveau, R. Brain Res. Dev. Brain Res. (2001) [Pubmed]
  5. Genetic response to DNA damage: proapoptotic targets of RhoB include modules for p53 response and susceptibility to Alzheimer's disease. Kamasani, U., Prendergast, G.C. Cancer Biol. Ther. (2005) [Pubmed]
  6. Phosphorylation-dependent and constitutive activation of Rho proteins by wild-type and oncogenic Vav-2. Schuebel, K.E., Movilla, N., Rosa, J.L., Bustelo, X.R. EMBO J. (1998) [Pubmed]
  7. Normal thyroid structure and function in rhophilin 2-deficient mice. Behrends, J., Clément, S., Pajak, B., Pohl, V., Maenhaut, C., Dumont, J.E., Schurmans, S. Mol. Cell. Biol. (2005) [Pubmed]
  8. RhoB is dispensable for mouse development, but it modifies susceptibility to tumor formation as well as cell adhesion and growth factor signaling in transformed cells. Liu, A.X., Rane, N., Liu, J.P., Prendergast, G.C. Mol. Cell. Biol. (2001) [Pubmed]
  9. Farnesylated RhoB inhibits radiation-induced mitotic cell death and controls radiation-induced centrosome overduplication. Milia, J., Teyssier, F., Dalenc, F., Ader, I., Delmas, C., Pradines, A., Lajoie-Mazenc, I., Baron, R., Bonnet, J., Cohen-Jonathan, E., Favre, G., Toulas, C. Cell Death Differ. (2005) [Pubmed]
  10. Cyclin B1 is a critical target of RhoB in the cell suicide program triggered by farnesyl transferase inhibition. Kamasani, U., Huang, M., Duhadaway, J.B., Prochownik, E.V., Donover, P.S., Prendergast, G.C. Cancer Res. (2004) [Pubmed]
  11. Differential translocation of rho family GTPases by lysophosphatidic acid, endothelin-1, and platelet-derived growth factor. Fleming, I.N., Elliott, C.M., Exton, J.H. J. Biol. Chem. (1996) [Pubmed]
  12. The ras-related small GTP-binding protein RhoB is immediate-early inducible by DNA damaging treatments. Fritz, G., Kaina, B., Aktories, K. J. Biol. Chem. (1995) [Pubmed]
  13. Isoprenylation of RhoB is necessary for its degradation. A novel determinant in the complex regulation of RhoB expression by the mevalonate pathway. Stamatakis, K., Cernuda-Morollón, E., Hernández-Perera, O., Pérez-Sala, D. J. Biol. Chem. (2002) [Pubmed]
  14. RhoB mRNA is stabilized by HuR after UV light. Westmark, C.J., Bartleson, V.B., Malter, J.S. Oncogene (2005) [Pubmed]
  15. RhoB and actin polymerization coordinate Src activation with endosome-mediated delivery to the membrane. Sandilands, E., Cans, C., Fincham, V.J., Brunton, V.G., Mellor, H., Prendergast, G.C., Norman, J.C., Superti-Furga, G., Frame, M.C. Dev. Cell (2004) [Pubmed]
  16. Selective expression of the small GTPase RhoB in the early developing mouse lens. Maddala, R., Peng, Y.W., Rao, P.V. Dev. Dyn. (2001) [Pubmed]
  17. GTPase RhoB: an early predictor of neuronal death after transient focal ischemia in mice. Trapp, T., Oláh, L., Hölker, I., Besselmann, M., Tiesler, C., Maeda, K., Hossmann, K.A. Mol. Cell. Neurosci. (2001) [Pubmed]
 
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