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Gene Review

NAB2  -  NGFI-A binding protein 2 (EGR1 binding...

Homo sapiens

Synonyms: EGR-1-binding protein 2, MADER, Melanoma-associated delayed early response protein, NGFI-A-binding protein 2, Protein MADER
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Disease relevance of NAB2


High impact information on NAB2

  • Cotransfection with p21(WAF1) restored the ability of NAB2-overexpressing PC12 cells to differentiate in response to NGF [5].
  • Furthermore, NAB2 overexpression led to downregulation of p21(WAF1), a molecule previously shown to play a pivotal role in the ability of PC12 cells to undergo growth arrest and commit to differentiation in response to NGF [5].
  • Inhibition of PC12 differentiation by NAB2 overexpression was confirmed using two additional experimental approaches, transient transfection, and adenoviral infection [5].
  • Furthermore, overexpression of NAB2, a corepressor of EGR-1, inhibited effects of OxPAPC [6].
  • We have isolated and characterized another corepressor, NAB2, which is highly related to NAB1 within two discrete domains [7].

Biological context of NAB2


Anatomical context of NAB2

  • Taken together, our findings identify NAB2 as a novel coactivator of T cell function [11].
  • Although Mader mRNA can be detected in most cell lines, only occasional immunoreactive cells were detected in normal human tissues [4].
  • Our results show that Mader is preferentially expressed on neurons and glial cells and that the adhesion protein MUC18/MCAM is mainly expressed on vasculature within the CNS [12].

Associations of NAB2 with chemical compounds

  • More recently, NO was shown to interact also with a mammalian 15-lipoxygenase [Wiesner, R., Rathmann, J., Holzhütter, H. G., Stosser, R., Mader, K., Nolting, H. & Kühn, H. (1996) Nitric oxide oxidises ferrous mammalian lipoxygenases to a pre-activated ferric species, FEBS Lett. 389, 229-232] [13].
  • The present study examined the relationship between lactic acid concentration in capillary blood and swimming velocity during 11 typical endurance exercises (continuous swimming for 30 and 60 min, interval swimming with distances between 50 and 400 m, and with rest periods of 10 and 30 s) and during the "two-speed test" recently described by Mader [14].
  • (1996) (Water Res. 30, 3130-3138) for sorption of toluene, ethylbenzenes, and xylenes onto the sediments from Belgian Continental Shelf and North Sea, as well as Mader et al [15].

Regulatory relationships of NAB2

  • During the initial phase EGR-1 is rapidly induced and NAB2 levels are down-regulated [8].
  • Both isoforms of NAB2 induced by FGF23 were localized in the nucleus and suppressed the transcriptional activity of Egr-1 [16].

Other interactions of NAB2

  • Firstly, we show a reciprocal regulation of EGR-1 and NAB2 following VEGF treatment [8].
  • This is followed by a reduction of EGR-1 and a concomitant increase of NAB2 [8].
  • Therefore, we hypothesized that mutations in the EGR2-interacting domains of NAB1 and NAB2 might be associated with the pathogenesis of inherited peripheral neuropathies in currently unexplained cases [1].
  • Expression of a wild-type NAB2 but not a dominant negative NAB2 mutant abrogates Egr-1 driven TF promoter activity and tubule formation in an in vitro model of angiogenesis [17].
  • Using stable transformants derived from MCF-7 cells which were transfected with expression-controllable Egr3-expression vector, we demonstrated that Nab2 is one of the target genes for EGR3 [18].

Analytical, diagnostic and therapeutic context of NAB2


  1. Search for mutations in the EGR2 corepressor proteins, NAB1 and NAB2, in human peripheral neuropathies. Venken, K., Di Maria, E., Bellone, E., Balestra, P., Cassandrini, D., Mandich, P., De Jonghe, P., Timmerman, V., Svaren, J. Neurogenetics (2002) [Pubmed]
  2. Frequent and early loss of the EGR1 corepressor NAB2 in human prostate carcinoma. Abdulkadir, S.A., Carbone, J.M., Naughton, C.K., Humphrey, P.A., Catalona, W.J., Milbrandt, J. Hum. Pathol. (2001) [Pubmed]
  3. Discovering biomarkers from gene expression data for predicting cancer subgroups using neural networks and relational fuzzy clustering. Pal, N.R., Aguan, K., Sharma, A., Amari, S. BMC Bioinformatics (2007) [Pubmed]
  4. Mader: a novel nuclear protein over expressed in human melanomas. Kirsch, K.H., Korradi, Y., Johnson, J.P. Oncogene (1996) [Pubmed]
  5. The transcriptional corepressor NAB2 inhibits NGF-induced differentiation of PC12 cells. Qu, Z., Wolfraim, L.A., Svaren, J., Ehrengruber, M.U., Davidson, N., Milbrandt, J. J. Cell Biol. (1998) [Pubmed]
  6. Oxidized phospholipids stimulate tissue factor expression in human endothelial cells via activation of ERK/EGR-1 and Ca(++)/NFAT. Bochkov, V.N., Mechtcheriakova, D., Lucerna, M., Huber, J., Malli, R., Graier, W.F., Hofer, E., Binder, B.R., Leitinger, N. Blood (2002) [Pubmed]
  7. NAB2, a corepressor of NGFI-A (Egr-1) and Krox20, is induced by proliferative and differentiative stimuli. Svaren, J., Sevetson, B.R., Apel, E.D., Zimonjic, D.B., Popescu, N.C., Milbrandt, J. Mol. Cell. Biol. (1996) [Pubmed]
  8. NAB2, a corepressor of EGR-1, inhibits vascular endothelial growth factor-mediated gene induction and angiogenic responses of endothelial cells. Lucerna, M., Mechtcheriakova, D., Kadl, A., Schabbauer, G., Schäfer, R., Gruber, F., Koshelnick, Y., Müller, H.D., Issbrücker, K., Clauss, M., Binder, B.R., Hofer, E. J. Biol. Chem. (2003) [Pubmed]
  9. NAB2 represses transcription by interacting with the CHD4 subunit of the nucleosome remodeling and deacetylase (NuRD) complex. Srinivasan, R., Mager, G.M., Ward, R.M., Mayer, J., Svaren, J. J. Biol. Chem. (2006) [Pubmed]
  10. Egr-1 induces the expression of its corepressor nab2 by activation of the nab2 promoter thereby establishing a negative feedback loop. Kumbrink, J., Gerlinger, M., Johnson, J.P. J. Biol. Chem. (2005) [Pubmed]
  11. Cutting Edge: TCR-Induced NAB2 Enhances T Cell Function by Coactivating IL-2 Transcription. Collins, S., Wolfraim, L.A., Drake, C.G., Horton, M.R., Powell, J.D. J. Immunol. (2006) [Pubmed]
  12. Melanoma-associated adhesion molecule MUC18/MCAM (CD146) and transcriptional regulator mader in normal human CNS. Schwarz, M.J., Müller, N., Körschenhausen, D., Kirsch, K.H., Penning, R., Ackenheil, M., Johnson, J.P., Hampel, H. Neuroimmunomodulation (1998) [Pubmed]
  13. A kinetic model for the interaction of nitric oxide with a mammalian lipoxygenase. Holzhütter, H.G., Wiesner, R., Rathmann, J., Stösser, R., Kühn, H. Eur. J. Biochem. (1997) [Pubmed]
  14. Relationship between swimming velocity and lactic concentration during continuous and intermittent training exercises. Olbrecht, J., Madsen, O., Mader, A., Liesen, H., Hollmann, W. International journal of sports medicine. (1985) [Pubmed]
  15. QSAR models to predict effect of ionic strength on sorption of chlorinated benzenes and phenols at sediment-water interface. Rao, B.H., Asolekar, S.R. Water Res. (2001) [Pubmed]
  16. FGF23 induces expression of two isoforms of NAB2, which are corepressors of Egr-1. Fukuda, T., Kanomata, K., Nojima, J., Urakawa, I., Suzawa, T., Imada, M., Kukita, A., Kamijo, R., Yamashita, T., Katagiri, T. Biochem. Biophys. Res. Commun. (2007) [Pubmed]
  17. The transcriptional corepressor NAB2 blocks Egr-1-mediated growth factor activation and angiogenesis. Houston, P., Campbell, C.J., Svaren, J., Milbrandt, J., Braddock, M. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  18. Transcription factor EGR3 is involved in the estrogen-signaling pathway in breast cancer cells. Inoue, A., Omoto, Y., Yamaguchi, Y., Kiyama, R., Hayashi, S.I. J. Mol. Endocrinol. (2004) [Pubmed]
  19. A Burkitt lymphoma cell line with integrated Epstein-Barr virus at a stable chromosome modification site. Popescu, N.C., Chen, M.C., Simpson, S., Solinas, S., DiPaolo, J.A. Virology (1993) [Pubmed]
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