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COPS8  -  COP9 signalosome subunit 8

Homo sapiens

Synonyms: COP9, COP9 homolog, COP9 signalosome complex subunit 8, CSN8, JAB1-containing signalosome subunit 8, ...
 
 
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Disease relevance of COPS8

 

High impact information on COPS8

  • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage [2].
  • One of the other subunits is COP11, mutations in which result in a phenotype identical to cop9 mutants [3].
  • During the biogenesis of the COP9 complex, a certain degree of prior subunit association is a prerequisite for proper nuclear translocation [3].
  • Three structurally related protein complexes, the COP9 signalosome, the proteasome lid, and the eukaryotic translation initiation factor 3, are revealing new insights into developmental processes and into cell cycle control in healthy cells and cells exposed to genotoxic stress [4].
  • The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases [5]?
 

Biological context of COPS8

  • The subunit 1 of the COP9 signalosome suppresses gene expression through its N-terminal domain and incorporates into the complex through the PCI domain [6].
  • COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system [7].
  • The purified complex contains COP9 and COP11 protein homologs and is very similar, if not identical, to the plant COP9 complex involved in light-mediated signal transduction [8].
  • Subunits of the COP9 complex include regulators of the Jun N-terminal kinase (JNK) and c-Jun, a nuclear hormone receptor binding protein and a cell-cycle regulator [9].
  • This finding indicates that over-expression of a functional subunit 1 or subunit 8 of the COP9 signalosome confers a gain-of-function phenotype relative to the complex [10].
 

Anatomical context of COPS8

  • These polypeptides of the 19S regulator form a reversibly binding subcomplex called the 'lid'. We isolated the 'lid' from human red blood cells and compared it with the COP9 signalosome complex [11].
  • Intracellular IL-1 receptor antagonist type 1 inhibits IL-1-induced cytokine production in keratinocytes through binding to the third component of the COP9 signalosome [12].
 

Other interactions of COPS8

  • In this study, we dissected structure and function of the subunit 1 (CSN1 or GPS1) of the COP9 signalosome relative to the complex [6].
  • Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome [13].
 

Analytical, diagnostic and therapeutic context of COPS8

  • However, eIF3e and eIF3b cofractionated by gel filtration chromatography in a complex that was larger than the COP9 signalosome [14].
  • Electron microscopy and subunit-subunit interaction studies reveal a first architecture of COP9 signalosome [15].
  • Several paraproteasomal mechanisms may influence the trafficking of ubiquitinated proteins and their interaction with the proteasome, including the expression and activity of the COP9 signalosome, the carboxy terminus of heat shock protein 70-interacting protein (CHIP) and valosin-containing protein (VCP) [16].

References

  1. Retinoblastoma Protein Regulation by the COP9 Signalosome. Ullah, Z., Buckley, M.S., Arnosti, D.N., Henry, R.W. Mol. Biol. Cell (2007) [Pubmed]
  2. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Groisman, R., Polanowska, J., Kuraoka, I., Sawada, J., Saijo, M., Drapkin, R., Kisselev, A.F., Tanaka, K., Nakatani, Y. Cell (2003) [Pubmed]
  3. The COP9 complex, a novel multisubunit nuclear regulator involved in light control of a plant developmental switch. Chamovitz, D.A., Wei, N., Osterlund, M.T., von Arnim, A.G., Staub, J.M., Matsui, M., Deng, X.W. Cell (1996) [Pubmed]
  4. Life is degrading--thanks to some zomes. von Arnim, A.G., Schwechheimer, C. Mol. Cell (2006) [Pubmed]
  5. The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases? Wolf, D.A., Zhou, C., Wee, S. Nat. Cell Biol. (2003) [Pubmed]
  6. The subunit 1 of the COP9 signalosome suppresses gene expression through its N-terminal domain and incorporates into the complex through the PCI domain. Tsuge, T., Matsui, M., Wei, N. J. Mol. Biol. (2001) [Pubmed]
  7. COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. Bech-Otschir, D., Kraft, R., Huang, X., Henklein, P., Kapelari, B., Pollmann, C., Dubiel, W. EMBO J. (2001) [Pubmed]
  8. A novel protein complex involved in signal transduction possessing similarities to 26S proteasome subunits. Seeger, M., Kraft, R., Ferrell, K., Bech-Otschir, D., Dumdey, R., Schade, R., Gordon, C., Naumann, M., Dubiel, W. FASEB J. (1998) [Pubmed]
  9. The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex. Wei, N., Tsuge, T., Serino, G., Dohmae, N., Takio, K., Matsui, M., Deng, X.W. Curr. Biol. (1998) [Pubmed]
  10. A gain-of-function phenotype conferred by over-expression of functional subunits of the COP9 signalosome in Arabidopsis. Kang, D., Wang, X., Cao, K., Sun, C., Deng, X.W., Wei, N. Plant J. (2000) [Pubmed]
  11. Comparison of human COP9 signalsome and 26S proteasome lid'. Henke, W., Ferrell, K., Bech-Otschir, D., Seeger, M., Schade, R., Jungblut, P., Naumann, M., Dubiel, W. Mol. Biol. Rep. (1999) [Pubmed]
  12. Intracellular IL-1 receptor antagonist type 1 inhibits IL-1-induced cytokine production in keratinocytes through binding to the third component of the COP9 signalosome. Banda, N.K., Guthridge, C., Sheppard, D., Cairns, K.S., Muggli, M., Bech-Otschir, D., Dubiel, W., Arend, W.P. J. Immunol. (2005) [Pubmed]
  13. Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome. Uhle, S., Medalia, O., Waldron, R., Dumdey, R., Henklein, P., Bech-Otschir, D., Huang, X., Berse, M., Sperling, J., Schade, R., Dubiel, W. EMBO J. (2003) [Pubmed]
  14. Arabidopsis eIF3e (INT-6) associates with both eIF3c and the COP9 signalosome subunit CSN7. Yahalom, A., Kim, T.H., Winter, E., Karniol, B., von Arnim, A.G., Chamovitz, D.A. J. Biol. Chem. (2001) [Pubmed]
  15. Electron microscopy and subunit-subunit interaction studies reveal a first architecture of COP9 signalosome. Kapelari, B., Bech-Otschir, D., Hegerl, R., Schade, R., Dumdey, R., Dubiel, W. J. Mol. Biol. (2000) [Pubmed]
  16. Molecular regulation of muscle cachexia: it may be more than the proteasome. Hasselgren, P.O., Wray, C., Mammen, J. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
 
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