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

CLSPN  -  claspin

Homo sapiens

Synonyms: Claspin, hClaspin
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of CLSPN

  • To this end, a monoclonal antibody was generated and the expression of claspin was investigated in normal fibroblasts and various cancer cell lines, as well as in tumour and normal tissues from patients with primary epithelial carcinomas [1].
 

High impact information on CLSPN

 

Biological context of CLSPN

 

Anatomical context of CLSPN

 

Associations of CLSPN with chemical compounds

 

Physical interactions of CLSPN

  • Significantly, expression of a stable Claspin mutant unable to bind betaTrCP prolongs the activation of Chk1, thereby attenuating the recovery from the DNA replication stress response and significantly delaying entry into mitosis [3].
 

Enzymatic interactions of CLSPN

  • Repeated phosphopeptide motifs in human claspin are phosphorylated by chk1 and mediate claspin function [7].
 

Regulatory relationships of CLSPN

 

Other interactions of CLSPN

  • Claspin localizes in the nuclei, but it only associates with Chk1 following replication stress or other types of DNA damage [8].
  • Claspin is an essential protein for the ATR-dependent activation of the DNA replication checkpoint response in Xenopus and human cells [9].
  • Moreover, Chk1 and Claspin promoter activities were also reduced after incubation with 1,25(OH)(2)D(3), and this reduction was mediated through the E2F recognition motifs within their promoters because mutation of these motifs almost completely abolished the repressive effect of 1,25(OH)(2)D(3) [10].
  • We found that during recovery from the DNA replication checkpoint response, Claspin is degraded in a betaTrCP-dependent manner [3].

References

  1. Evaluation of claspin as a proliferation marker in human cancer and normal tissues. Tsimaratou, K., Kletsas, D., Kastrinakis, N., Tsantoulis, P., Evangelou, K., Sideridou, M., Liontos, M., Poulias, I., Venere, M., Salmas, M., Kittas, C., Halazonetis, T., Gorgoulis, V. J. Pathol. (2007) [Pubmed]
  2. Rad17 phosphorylation is required for claspin recruitment and Chk1 activation in response to replication stress. Wang, X., Zou, L., Lu, T., Bao, S., Hurov, K.E., Hittelman, W.N., Elledge, S.J., Li, L. Mol. Cell (2006) [Pubmed]
  3. SCFbetaTrCP-mediated degradation of Claspin regulates recovery from the DNA replication checkpoint response. Peschiaroli, A., Dorrello, N.V., Guardavaccaro, D., Venere, M., Halazonetis, T., Sherman, N.E., Pagano, M. Mol. Cell (2006) [Pubmed]
  4. Human Claspin works with BRCA1 to both positively and negatively regulate cell proliferation. Lin, S.Y., Li, K., Stewart, G.S., Elledge, S.J. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  5. DNA-dependent phosphorylation of Chk1 and Claspin in a human cell-free system. Clarke, C.A., Clarke, P.R. Biochem. J. (2005) [Pubmed]
  6. DNA-Damage Control: Claspin Destruction Turns off the Checkpoint. Gewurz, B.E., Harper, J.W. Curr. Biol. (2006) [Pubmed]
  7. Repeated phosphopeptide motifs in human claspin are phosphorylated by chk1 and mediate claspin function. Chini, C.C., Chen, J. J. Biol. Chem. (2006) [Pubmed]
  8. Human claspin is required for replication checkpoint control. Chini, C.C., Chen, J. J. Biol. Chem. (2003) [Pubmed]
  9. Human claspin is a ring-shaped DNA-binding protein with high affinity to branched DNA structures. Sar, F., Lindsey-Boltz, L.A., Subramanian, D., Croteau, D.L., Hutsell, S.Q., Griffith, J.D., Sancar, A. J. Biol. Chem. (2004) [Pubmed]
  10. 1alpha,25-Dihydroxyvitamin D(3)-induced down-regulation of the checkpoint proteins, Chk1 and Claspin, is mediated by the pocket proteins p107 and p130. Verlinden, L., Eelen, G., Van Hellemont, R., Engelen, K., Beullens, I., Van Camp, M., Marchal, K., Mathieu, C., Bouillon, R., Verstuyf, A. J. Steroid Biochem. Mol. Biol. (2007) [Pubmed]
 
WikiGenes - Universities