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Gene Review

Synj2bp  -  synaptojanin 2 binding protein

Mus musculus

Synonyms: AA409442, ARIP2, ARIP2a, ActRIP4, Activin receptor-interacting protein 2, ...
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Disease relevance of Synj2bp

  • The 28-kDa protein had a primary amino acid sequence that was 43% similar to a previously described Brucella abortus group 3 Ag, Omp25 (P. de Wergifosse, P. Lintermans, J. N. Limet, and A. Cloeckaert, J. Bacteriol. 177:1911-1914, 1995) [1].
  • The specificity to Omp25 of murine antibodies induced by E. coli (pAC2533) was demonstrated by SDS-PAGE and immunoblotting of five B. melitensis strains [2].
  • To aid in the development of novel efficacious vaccines against brucellosis, Omp25 was examined as a potential candidate [3].

High impact information on Synj2bp

  • Overexpression of OMP25 results in perinuclear clustering of mitochondria in transfected cells [4].
  • Moreover, we have identified that the COOH-terminal region of ARIP2 interacts with Ral-binding protein 1 (RalBP1) [5].
  • Interestingly, overexpression of ARIP2 enhances endocytosis of ActRIIs and reduces activin-induced transcription in Chinese hamster ovary K1 cells [5].
  • The recent release of the genome sequence of B. melitensis 16 M has revealed the presence of five additional gene products homologous to Omp25 and Omp31 [6].
  • The data from the present study, together with previous results, suggest that humoral immunity against probably conformational, well-exposed epitopes of the Omp25 could contribute to protective mechanisms against B. melitensis infection in mice [2].

Biological context of Synj2bp

  • Overexpression of ARIP2 enhances endocytosis of ActRIIs [7].
  • Groups of mice were immunised and boosted either with sonicated E. coli carrying plasmid pAC2533-E. coli (pAC2533)-expressing the gene coding for Omp25 (omp25 gene) of B. melitensis, or with E. coli carrying plasmid pUC19-E. coli (pUC19) [2].

Anatomical context of Synj2bp


Associations of Synj2bp with chemical compounds

  • Only denaturing SDS-gel filtration chromatography was able to separate proteins of about 29 kDa from rough lipopolysaccharide but did not separate Omp31 from Omp25 in B. ovis preparations [9].

Analytical, diagnostic and therapeutic context of Synj2bp

  • In addition, immunofluorescence co-localization studies indicated the direct involvement of ARIP2 in the intracellular translocation of ActRIIs by PDZ domain-mediated interaction [5].
  • The Omp25 antigen (BMEI1249) has previously been studied in terms of Brucella virulence, serodiagnosis and as a protective antigen [10].
  • Mutants lacking Omp25 are indeed attenuated in animal models of infection, and moreover provide levels of protection similar or better than currently used attenuated vaccine strain B. melitensis Rev.1. Therefore, these mutant strains appear interesting vaccine candidates for the future [6].
  • Western immunoblot analysis and PCR verified that the Omp25 protein was not expressed and that the omp25 gene was disrupted in each strain [3].


  1. Cloning of a Brucella melitensis group 3 antigen gene encoding Omp28, a protein recognized by the humoral immune response during human brucellosis. Lindler, L.E., Hadfield, T.L., Tall, B.D., Snellings, N.J., Rubin, F.A., Van De Verg, L.L., Hoover, D., Warren, R.L. Infect. Immun. (1996) [Pubmed]
  2. Evaluation of immunogenicity and protective activity in BALB/c mice of the 25-kDa major outer-membrane protein of Brucella melitensis (Omp25) expressed in Escherichia coli. Bowden, R.A., Cloeckaert, A., Zygmunt, M.S., Dubray, G. J. Med. Microbiol. (1998) [Pubmed]
  3. Brucella species lacking the major outer membrane protein Omp25 are attenuated in mice and protect against Brucella melitensis and Brucella ovis. Edmonds, M.D., Cloeckaert, A., Elzer, P.H. Vet. Microbiol. (2002) [Pubmed]
  4. Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein. Nemoto, Y., De Camilli, P. EMBO J. (1999) [Pubmed]
  5. Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway. Matsuzaki, T., Hanai, S., Kishi, H., Liu, Z., Bao, Y., Kikuchi, A., Tsuchida, K., Sugino, H. J. Biol. Chem. (2002) [Pubmed]
  6. Major outer membrane proteins of Brucella spp.: past, present and future. Cloeckaert, A., Vizcaíno, N., Paquet, J.Y., Bowden, R.A., Elzer, P.H. Vet. Microbiol. (2002) [Pubmed]
  7. Novel factors in regulation of activin signaling. Tsuchida, K., Nakatani, M., Matsuzaki, T., Yamakawa, N., Liu, Z., Bao, Y., Arai, K.Y., Murakami, T., Takehara, Y., Kurisaki, A., Sugino, H. Mol. Cell. Endocrinol. (2004) [Pubmed]
  8. Effects of activin A on the activities of the mouse peritoneal macrophages. Zhang, X.J., Li, Y., Tai, G.X., Xu, G.Y., Zhang, P.Y., Yang, Y., Lao, F.X., Liu, Z.H. Cell. Mol. Immunol. (2005) [Pubmed]
  9. Characterization of an immuno-dominant antigen in Brucella ovis and evaluation of its use in an enzyme-linked immunosorbent assay. Kittelberger, R., Diack, D.S., Vizcaíno, N., Zygmunt, M.S., Cloeckaert, A. Vet. Microbiol. (1998) [Pubmed]
  10. The identification of two protective DNA vaccines from a panel of five plasmid constructs encoding Brucella melitensis 16M genes. Commander, N.J., Spencer, S.A., Wren, B.W., Macmillan, A.P. Vaccine (2007) [Pubmed]
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