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NDRG4  -  NDRG family member 4

Homo sapiens

Synonyms: BDM1, Brain development-related molecule 1, KIAA1180, N-myc downstream-regulated gene 4 protein, Protein NDRG4, ...
 
 
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High impact information on NDRG4

 

Biological context of NDRG4

  • The full-length smap8 cDNA is 3241 bp long and contains an open reading frame of 1113 bp encoding an approximately 45 kDa soluble protein identical to NDRG4 protein [3].
  • Based on UniGene cluster analysis, the genes NDRG2, NDRG3 and NDRG4 are located at chromosome 14q11.1-11.2, 20q12-11.23 and 16q21-22.1, respectively [4].
  • PDGF was the most prominent in promoting phosphorylation of the smap8 protein [3].
  • The BDM-1 deduced amino acid sequence contained several significant clusters of identity with mammalian phosducin, including a domain corresponding to a highly conserved 11-amino acid stretch that has been implicated in binding to the Gbetagamma dimer and two regions of defined Gbeta/phosducin contact points [1].
  • Ndrg4 is expressed predominantly in the early postnatal rat brain and may be related to neural cell differentiation [5].
 

Anatomical context of NDRG4

  • In contrast, the NDRG4 protein-highly expressing clones did not show suppressed neurite outgrowth induced by NGF [6].
  • An antisense construct of rat NDRG4 cDNA was made and transfected to PC12 cells, which constitutively express a basal level of the NDRG4 protein [6].
  • Smap8 mRNA was expressed predominantly in the brain and heart, and moderately in vascular smooth muscle cells [3].
  • We isolated the cDNA of a gene, designated smooth muscle-associated protein 8 (smap8), during a search for new genes expressed in human aortic smooth muscle cells [3].
  • The suppressive effect of Ndrg4-C2 on NGF-induced activation of Elk-1 was abolished by colchicine but not by cytochalasin D, suggesting that microtubules are involved in the reduced activation of Elk-1 by Ndrg4 [5].
 

Associations of NDRG4 with chemical compounds

 

Regulatory relationships of NDRG4

  • Ndrg4 enhances NGF-induced ERK activation uncoupled with Elk-1 activation [5].
 

Other interactions of NDRG4

  • Characterization of the human NDRG gene family: a newly identified member, NDRG4, is specifically expressed in brain and heart [2].
  • Ndrg4 may play a role in supporting the activation of ERK and its target proteins needed for neuronal differentiation and in reducing the activation of Elk-1 implicated in cell growth [5].
 

Analytical, diagnostic and therapeutic context of NDRG4

  • We show, by sequence analysis and fold recognition methods, that Bdm1 has strong structural similarities to alpha/beta hydrolases like the thioesterases [7].

References

  1. Identification of bdm-1, a gene involved in G protein beta-subunit function and alpha-subunit accumulation. Kasahara, S., Wang, P., Nuss, D.L. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  2. Characterization of the human NDRG gene family: a newly identified member, NDRG4, is specifically expressed in brain and heart. Zhou, R.H., Kokame, K., Tsukamoto, Y., Yutani, C., Kato, H., Miyata, T. Genomics (2001) [Pubmed]
  3. A novel homocysteine-responsive gene, smap8, modulates mitogenesis in rat vascular smooth muscle cells. Nishimoto, S., Tawara, J., Toyoda, H., Kitamura, K., Komurasaki, T. Eur. J. Biochem. (2003) [Pubmed]
  4. Characterization and expression of three novel differentiation-related genes belong to the human NDRG gene family. Qu, X., Zhai, Y., Wei, H., Zhang, C., Xing, G., Yu, Y., He, F. Mol. Cell. Biochem. (2002) [Pubmed]
  5. Ndrg4 enhances NGF-induced ERK activation uncoupled with Elk-1 activation. Hongo, S., Watanabe, T., Takahashi, K., Miyazaki, A. J. Cell. Biochem. (2006) [Pubmed]
  6. Inhibition of neurite outgrowth by reduced level of NDRG4 protein in antisense transfected PC12 cells. Ohki, T., Hongo, S., Nakada, N., Maeda, A., Takeda, M. Brain Res. Dev. Brain Res. (2002) [Pubmed]
  7. Fold prediction and comparative modeling of Bdm1: a probable alpha/beta hydrolase associated with hot water epilepsy. Bhaduri, A., Krishnaswamy, L., Ullal, G.R., Panicker, M.R., Sowdhamini, R. Journal of molecular modeling (Online) (2003) [Pubmed]
 
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