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Gene Review

RHOBTB2  -  Rho-related BTB domain containing 2

Homo sapiens

Synonyms: DBC2, Deleted in breast cancer 2 gene protein, KIAA0717, Rho-related BTB domain-containing protein 2, p83
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Disease relevance of RHOBTB2

  • Unlike other genes in the region, expression of DBC2 is often extinguished in breast cancer cells or tissues [1].
  • DBC2 is Essential for Transporting Vesicular Stomatitis Virus Glycoprotein [2].
  • DBC2 is a tumor suppressor gene linked to breast and lung cancers [2].
  • Sera from patients with early or late symptoms of Lyme borreliosis contained antibodies of various classes against about 80 antigens each, containing the already described antigens OspA, B and C, flagellin, p83/100, and p39 [3].
  • The slower sedimenting component (190S-1) contained p88 and p83 as the major capsid proteins; the faster component (190S-2) contained p88 and p78 [4].

High impact information on RHOBTB2


Chemical compound and disease context of RHOBTB2

  • Furthermore, when Western blots of capsid polypeptides were reacted with an antiserum to glutaraldehyde-stabilized virus (190S-G), p88 was more reactive to 190S-G antibodies than was p83/p78 [6].
  • Selective chemical cleavage at tryptophan residues of in vitro 32P-labeled capsid proteins revealed four labeled peptides among the cleavage products of both p83 and p88 [4].

Biological context of RHOBTB2


Anatomical context of RHOBTB2

  • DBC2 was introduced into HeLa cells by a mammalian expression vector with a constitutive promoter [8].
  • We demonstrate that DBC2 mobility depends also on an intact microtubule network [2].
  • We conclude that DBC2 plays an essential role in microtubule-mediated VSVG transport from the endoplasmic reticulum to the Golgi apparatus [2].
  • The finding of a somatic mutation of DBC2 in a tumour sample and the down-regulation of both gene transcripts in bladder tumour cell lines may indicate that an alternative mechanism of inactivation of the second allele, for example promoter hypermethylation, is more common than mutation and this must now be examined [9].
  • Since comparison of the p83/100 molecule with sequences from protein databases showed similarities with characteristics of eukaryotic cell structures, the p83/100 might mimic these structures and may, therefore, be involved in the immune escape mechanism of the pathogenic agent of Lyme disease [10].

Associations of RHOBTB2 with chemical compounds

  • Histamine increases 32P-incorporation into two acidic proteins of Mr 83,000 and of Mr 29,000, designated p83 and p29 [11].
  • Labeling of p83 and p29 is also increased in cells exposed to ionomycin, but not in cells exposed to vasoactive intestinal peptide under conditions resulting in cAMP-mediated secretion and cAMP-stimulated protein phosphorylation [11].
  • Increasing labeling of p83 parallels stimulated secretion with respect to the onset of agonist action, agonist potency, and antagonism by atropine [12].
  • During starvation (minus glutamine), three polyphosphate substances accumulated intracellularly, ATP was rapidly depleted, and a protein of molecular weight 42 000 (presumed to be actin) was actively synthesized, whereas synthesis of the most abundant detergent-soluble protein of molecular weight 83 000 (p83) ceased [13].
  • Phosphorylation of p83 also occurs when a T84 cell extract is incubated with purified protein kinase C and when intact cells are exposed to phorbol myristate acetate. p83 does not become phosphorylated in cell fractions incubated with adenosine 3',5'-cyclic monophosphate (cAMP) or in monolayers stimulated with agonists acting via cAMP [12].

Other interactions of RHOBTB2

  • By contrast, the exon-intron organization of RHOBTB3 differed substantially from that of the two other genes, indicating that this gene arose by a duplication event independent of the one that gave rise to RHOBTB1 and RHOBTB2 [7].
  • The biological roles of RHOBTB proteins, including DBC2, remain unclear [8].

Analytical, diagnostic and therapeutic context of RHOBTB2

  • VASP binding to purified p83 in solid-phase binding assays and the closely matching subcellular localization in double-label immunofluorescence analyses demonstrated that both proteins also directly interact as native proteins in vitro and possibly in living cells [5].
  • Peptide mapping by both limited proteolysis and selective chemical cleavage showed p83 and p78 to be closely related to p88 [6].
  • The suitability of this new antigen for the diagnosis of Lyme disease was tested by immunoblotting; for comparison, the recombinant variable region of the flagellin, the 18-kDa fragment (p18), and the whole recombinant 83-kDa protein (p83), both expressed in E. coli, were used [14].
  • To study the structure of this heterogeneous region, and internal fragment of the p83/100 genes from 11 additional B. burgdorferi sensu lato strains was amplified by PCR [10].
  • Cluster analysis of internal p83/100 fragments, as well as restriction enzyme analysis, revealed three major groups in accordance with grouping into the three species causing Lyme disease [10].


  1. DBC2, a candidate for a tumor suppressor gene involved in breast cancer. Hamaguchi, M., Meth, J.L., von Klitzing, C., Wei, W., Esposito, D., Rodgers, L., Walsh, T., Welcsh, P., King, M.C., Wigler, M.H. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  2. DBC2 is Essential for Transporting Vesicular Stomatitis Virus Glycoprotein. Chang, F.K., Sato, N., Kobayashi-Simorowski, N., Yoshihara, T., Meth, J.L., Hamaguchi, M. J. Mol. Biol. (2006) [Pubmed]
  3. Proteomics in human disease: cancer, heart and infectious diseases. Jungblut, P.R., Zimny-Arndt, U., Zeindl-Eberhart, E., Stulik, J., Koupilova, K., Pleissner, K.P., Otto, A., Müller, E.C., Sokolowska-Köhler, W., Grabher, G., Stöffler, G. Electrophoresis (1999) [Pubmed]
  4. The Helminthosporium victoriae 190S mycovirus has two forms distinguishable by capsid protein composition and phosphorylation state. Ghabrial, S.A., Havens, W.M. Virology (1992) [Pubmed]
  5. Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Reinhard, M., Jouvenal, K., Tripier, D., Walter, U. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  6. The capsid polypeptides of the 190S virus of Helminthosporium victoriae. Ghabrial, S.A., Bibb, J.A., Price, K.H., Havens, W.M., Lesnaw, J.A. J. Gen. Virol. (1987) [Pubmed]
  7. Genomic organization and expression profile of the small GTPases of the RhoBTB family in human and mouse. Ramos, S., Khademi, F., Somesh, B.P., Rivero, F. Gene (2002) [Pubmed]
  8. DBC2 significantly influences cell-cycle, apoptosis, cytoskeleton and membrane-trafficking pathways. Siripurapu, V., Meth, J., Kobayashi, N., Hamaguchi, M. J. Mol. Biol. (2005) [Pubmed]
  9. Mutation analysis of the 8p candidate tumour suppressor genes DBC2 (RHOBTB2) and LZTS1 in bladder cancer. Knowles, M.A., Aveyard, J.S., Taylor, C.F., Harnden, P., Bass, S. Cancer Lett. (2005) [Pubmed]
  10. Molecular and immunological characterization of the p83/100 protein of various Borrelia burgdorferi sensu lato strains. Rössler, D., Eiffert, H., Jauris-Heipke, S., Lehnert, G., Preac-Mursic, V., Teepe, J., Schlott, T., Soutschek, E., Wilske, B. Med. Microbiol. Immunol. (Berl.) (1995) [Pubmed]
  11. Histamine stimulates calcium-mediated protein phosphorylation in a colonic epithelial cell line. Cohn, J.A., Dougherty, N.C., King, W.F. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  12. Protein kinase C mediates cholinergically regulated protein phosphorylation in a Cl(-)-secreting epithelium. Cohn, J.A. Am. J. Physiol. (1990) [Pubmed]
  13. L-glutamine alteration of gene expression, not of polyphosphate and calcium metabolism, is a key event in arresting fungal sporulation. LéJohn, H.B. Can. J. Biochem. Cell Biol. (1983) [Pubmed]
  14. Use of a hybrid protein consisting of the variable region of the Borrelia burgdorferi flagellin and part of the 83-kDa protein as antigen for serodiagnosis of Lyme disease. Rasiah, C., Rauer, S., Gassmann, G.S., Vogt, A. J. Clin. Microbiol. (1994) [Pubmed]
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