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

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Gene Review: 

PSMA3  -  proteasome (prosome, macropain) subunit,...

Homo sapiens

Synonyms: HC8, Macropain subunit C8, Multicatalytic endopeptidase complex subunit C8, PSC3, PSC8, ...
 
 
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High impact information on PSMA3

  • Hyperfine couplings to HC8 and HC2 were fully characterized with ENDOR spectroscopy, and the identification was supported by DFT calculations [1].
  • Electrophoretic mobility shift assays revealed that BO-653-mediated induction of DNA-binding to an upstream promoter region of PSMA3 containing the ARE motif was blocked by antibody against c-Jun but not Nrf2 [2].
  • Two antioxidant responsive elements (AREs) were identified in the promoter region of proteasome alpha subunit 3 (PSMA3) [2].
  • Results from promoter truncation analysis revealed that the proximal ARE region was necessary for the down-regulation of the expression of PSMA3 [2].
  • We mapped the HC8 gene at q23 on human chromosome 14, which differs from the chromosomal locations of nine other proteasomal subunit genes mapped so far [3].
 

Biological context of PSMA3

  • Our data suggest that Aurora-B might undergo degradation by binding to HC8 in a proteasome-dependent manner during mitosis [4].
  • For study of the molecular basis of regulation of proteasome gene expression, we isolated the gene encoding the alpha-type HC8 subunit of the human proteasome [3].
 

Associations of PSMA3 with chemical compounds

  • R2 was the product of net hydrogen loss from N7, equivalent to the one-electron oxidation product of neutral hypoxanthine, and exhibited alpha-proton hyperfine couplings to HC2 and HC8 [5].
 

Physical interactions of PSMA3

  • Human aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner [4].
 

Other interactions of PSMA3

  • On the other hand, genes of three subunits of proteasome (PSMA2, PSMA3, PSMA4) were down-regulated by these antioxidants [6].

References

  1. EPR and ENDOR study of radiation-induced radical formation in purines: sodium inosine crystals X-irradiated at 10 K. Tokdemir, S., Nelson, W.H. The journal of physical chemistry. A, Molecules, spectroscopy, kinetics, environment & general theory. (2006) [Pubmed]
  2. Chemical structure-dependent gene expression of proteasome subunits via regulation of the antioxidant response element. Takabe, W., Matsukawa, N., Kodama, T., Tanaka, K., Noguchi, N. Free Radic. Res. (2006) [Pubmed]
  3. Isolation and characterization of the HC8 subunit gene of the human proteasome. Akioka, H., Forsberg, N.E., Ishida, N., Okumura, K., Nogami, M., Taguchi, H., Noda, C., Tanaka, K. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  4. Human aurora-B binds to a proteasome alpha-subunit HC8 and undergoes degradation in a proteasome-dependent manner. Shu, F., Guo, S., Dang, Y., Qi, M., Zhou, G., Guo, Z., Zhang, Y., Wu, C., Zhao, S., Yu, L. Mol. Cell. Biochem. (2003) [Pubmed]
  5. EPR and ENDOR study of radiation-induced radical formation in purines: hypoxanthine hydrochloride monohydrate crystals X-irradiated at 10 K. Tokdemir, S., Nelson, W.H. The journal of physical chemistry. A, Molecules, spectroscopy, kinetics, environment & general theory. (2005) [Pubmed]
  6. Gene expression induced by BO-653, probucol and BHQ in human endothelial cells. Takabe, W., Mataki, C., Wada, Y., Ishii, M., Izumi, A., Aburatani, H., Hamakubo, T., Niki, E., Kodama, T., Noguchi, N. J. Atheroscler. Thromb. (2000) [Pubmed]
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