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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

SYNJ2BP  -  synaptojanin 2 binding protein

Homo sapiens

Synonyms: ARIP2, Arip2, Mitochondrial outer membrane protein 25, OMP25, Synaptojanin-2-binding protein
 
 
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Disease relevance of SYNJ2BP

  • Thus, we have analyzed the effects of two major OMPs (Omp25 and Omp31) of Brucella suis 1330 (wild-type [WT] B. suis) on TNF-alpha production [1].
  • We demonstrate the production of three paralogs of Omp31 and/or Omp25 in B. suis, and the existence of a common site of signal peptide cleavage (AXAAD), which is very similar to that present in the five homologous Omps of Bartonella quintana [2].
 

High impact information on SYNJ2BP

  • Here, we analyzed the import route of mitochondrial outer membrane (MOM) C-TA proteins, Bak, Bcl-XL, and Omp25, using digitonin-permeabilized HeLa cells, which provide specific and efficient import under competitive conditions [3].
  • To test our observation that a peroxisomal location is not required for PEX26 function, we made a chimeric protein (PEX26-Mito) with PEX26 as its N-terminus and the targeting segment of a mitochondrial outer membrane protein (OMP25) at its C-terminus [4].
  • The seven group 3 Omps were classified in four-subgroups on the basis of percentage amino acid sequence identities: Omp25 alone, the Omp25b-Omp25c-Omp25d cluster, the Omp31/31b subgroup, and the less related Omp22 protein (also called Omp3b) [2].
  • These observations demonstrated that Omp25 of B. suis is involved in the negative regulation of TNF-alpha production upon infection of human macrophages [1].
  • Five genes homologous to the well-known omp25 and omp31 genes, that code for two major Brucella spp. outer membrane proteins (OMPs), have been detected in the genome of Brucella melitensis 16M and Brucella suis 1330 [5].
 

Chemical compound and disease context of SYNJ2BP

  • Latex beads coated with MAb to R-LPS coagglutinated only R strains, whereas latex beads coated with MAb to Omp25 coagglutinated all the R Brucella isolates except Brucella ovis [6].
 

Associations of SYNJ2BP with chemical compounds

  • Latex beads were coated, via protein A, with either an anti-Brucella rough-lipopolysaccharide (R-LPS) monoclonal antibody (MAb) or an anti-Brucella 25-kDa outer membrane protein (Omp25) MAb [6].
 

Analytical, diagnostic and therapeutic context of SYNJ2BP

  • Since several monoclonal antibodies (MAbs) against Omp25 cross-reacted with other members of group 3 Omps, we also performed Western immunoblotting to compare wild-type B. suis with mutants systematically having B. suis omp25-related genes knocked out [2].

References

  1. Major outer membrane protein Omp25 of Brucella suis is involved in inhibition of tumor necrosis factor alpha production during infection of human macrophages. Jubier-Maurin, V., Boigegrain, R.A., Cloeckaert, A., Gross, A., Alvarez-Martinez, M.T., Terraza, A., Liautard, J., Köhler, S., Rouot, B., Dornand, J., Liautard, J.P. Infect. Immun. (2001) [Pubmed]
  2. Characterization of new members of the group 3 outer membrane protein family of Brucella spp. Salhi, I., Boigegrain, R.A., Machold, J., Weise, C., Cloeckaert, A., Rouot, B. Infect. Immun. (2003) [Pubmed]
  3. Cytosolic factor- and TOM-independent import of C-tail-anchored mitochondrial outer membrane proteins. Setoguchi, K., Otera, H., Mihara, K. EMBO J. (2006) [Pubmed]
  4. Alternative splicing suggests extended function of PEX26 in peroxisome biogenesis. Weller, S., Cajigas, I., Morrell, J., Obie, C., Steel, G., Gould, S.J., Valle, D. Am. J. Hum. Genet. (2005) [Pubmed]
  5. DNA polymorphism in the omp25/omp31 family of Brucella spp.: identification of a 1.7-kb inversion in Brucella cetaceae and of a 15.1-kb genomic island, absent from Brucella ovis, related to the synthesis of smooth lipopolysaccharide. Vizcaíno, N., Caro-Hernández, P., Cloeckaert, A., Fernández-Lago, L. Microbes Infect. (2004) [Pubmed]
  6. Rapid identification of rough Brucella isolates by a latex coagglutination assay with the 25-kilodalton outer membrane protein and rough-lipopolysaccharide-specific monoclonal antibodies. Bowden, R.A., Verger, J.M., Grayon, M., Cloeckaert, A. Clin. Diagn. Lab. Immunol. (1997) [Pubmed]
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