The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

Links

 

Gene Review

RFWD2  -  ring finger and WD repeat domain 2, E3...

Homo sapiens

Synonyms: COP1, Constitutive photomorphogenesis protein 1 homolog, E3 ubiquitin-protein ligase RFWD2, FLJ10416, RING finger and WD repeat domain protein 2, ...
 
 
 

Disease relevance of RFWD2

 

High impact information on RFWD2

  • In plants, COP1 acts as an E3 ubiquitin ligase to repress light signaling by targeting photoreceptors and downstream transcription factors for ubiquitylation and degradation [2].
  • Using morphological, cellular, and gene expression criteria for epistasis analyses to position CR88 in the genetic hierarchy of the photomorphogenesis pathway, we determined that CR88 acts downstream of COP1 but in a branch separate from HY5 [3].
  • In the course of our analysis, we discovered that light causes extensive destruction of plastids in dark-grown cop1 seedlings and that cr88 prevents this destruction [3].
  • Genetic interactions between the chlorate-resistant mutant cr 8 8 and the photomorphogenic mutants cop1 and hy5 [3].
  • COP1, the negative regulator of p53, is overexpressed in breast and ovarian adenocarcinomas [1].
 

Associations of RFWD2 with chemical compounds

  • We suggest that by functioning as a FoxO1 E3 ligase, COP1 may play a role in the regulation of hepatic glucose metabolism [4].
 

Biological context of RFWD2

  • ATM engages autodegradation of the E3 ubiquitin ligase COP1 after DNA damage [5].
  • Through mutagenesis studies, we have defined a leucine-rich nuclear export signal (NES) within the coiled-coil domain of mammalian COP1 and a nuclear localization signal (NLS), which is composed of two clusters of positive-charged amino acids, bridged by the RING finger [6].
  • Furthermore, phosphorylation of COP1 on Ser(387) was required to permit p53 to become stabilized and to exert its tumor suppressor properties in response to DNA damage [5].
  • Depletion of COP1 by short interfering RNA (siRNA) stabilizes p53 and arrests cells in the G1 phase of the cell cycle [7].
  • Furthermore, we identify COP1 as a p53-inducible gene, and show that the depletion of COP1 and MDM2 by siRNA cooperatively sensitizes U2-OS cells to ionizing-radiation-induced cell death [7].
 

Associations of RFWD2 with chemical compounds

  • Mammalian COP1 contains a classic leucine-rich NES and a novel bipartite NLS bridged by a RING finger domain [6].
 

Enzymatic interactions of RFWD2

  • We observed that in response to DNA damage, ATM phosphorylated COP1 on Ser(387) and stimulated a rapid autodegradation mechanism [5].
 


References

  1. COP1, the negative regulator of p53, is overexpressed in breast and ovarian adenocarcinomas. Dornan, D., Bheddah, S., Newton, K., Ince, W., Frantz, G.D., Dowd, P., Koeppen, H., Dixit, V.M., French, D.M. Cancer Res. (2004) [Pubmed]
  2. COP1 - from plant photomorphogenesis to mammalian tumorigenesis. Yi, C., Deng, X.W. Trends Cell Biol. (2005) [Pubmed]
  3. Genetic interactions between the chlorate-resistant mutant cr 8 8 and the photomorphogenic mutants cop1 and hy5. Cao, D., Lin, Y., Cheng, C.L. Plant Cell (2000) [Pubmed]
  4. COP1 functions as a FoxO1 ubiquitin E3 ligase to regulate FoxO1-mediated gene expression. Kato, S., Ding, J., Pisck, E., Jhala, U.S., Du, K. J. Biol. Chem. (2008) [Pubmed]
  5. ATM engages autodegradation of the E3 ubiquitin ligase COP1 after DNA damage. Dornan, D., Shimizu, H., Mah, A., Dudhela, T., Eby, M., O'rourke, K., Seshagiri, S., Dixit, V.M. Science (2006) [Pubmed]
  6. An initial biochemical and cell biological characterization of the mammalian homologue of a central plant developmental switch, COP1. Yi, C., Wang, H., Wei, N., Deng, X.W. BMC Cell Biol. (2002) [Pubmed]
  7. The ubiquitin ligase COP1 is a critical negative regulator of p53. Dornan, D., Wertz, I., Shimizu, H., Arnott, D., Frantz, G.D., Dowd, P., O'Rourke, K., Koeppen, H., Dixit, V.M. Nature (2004) [Pubmed]
 
WikiGenes - Universities