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Gene Review:

clspn - claspin

Xenopus laevis

Yoo, H.Y. et al., Kumagai, A. et al., Lee, J. et al., Lee, J. et al., Yanow, S.K. et al., et al.

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High impact information on LOC398192

This interaction promotes the phosphorylation of Claspin on a nearby serine (S934) by Plx1 [1].
These results indicate that the Plx1-dependent inactivation of Claspin results in termination of a DNA replication checkpoint response [1].
By contrast, aphidicolin-treated extracts containing mutants of Claspin with alanine substitutions at positions 906 or 934 (T906A or S934A) are unable to undergo adaptation [1].
Conversely, neither phosphorylation of Claspin on these sites nor the presence of BRCA1 is necessary for activation of Chk1 in response to stalled replication forks [2].
We show here that Claspin associates with chromatin in a regulated manner during S phase [3].

Biological context of LOC398192

Immunodepletion of Claspin from egg extracts abolishes both the phosphorylation and activation of Xchk1 [4].
Furthermore, Claspin-depleted extracts are unable to arrest the cell cycle in response to DNA replication blocks [4].
Binding of Claspin to Xchk1 is highly elevated in the presence of DNA templates that trigger a checkpoint arrest of the cell cycle in Xenopus egg extracts [4].
These dependencies suggest that binding of Claspin occurs around the time of initial DNA unwinding at replication origins [3].

Associations of LOC398192 with chemical compounds

These observations suggest that the increased binding of Drf1 to aphidicolin-treated chromatin is an active process that is mediated by a caffeine-sensitive checkpoint pathway containing ATR and Claspin [5].

Other interactions of LOC398192

Phosphorylation of Xenopus Rad1 and Hus1 defines a readout for ATR activation that is independent of Claspin and the Rad9 carboxy terminus [6].
We show that Claspin contains a replication fork-interacting domain (RFID, residues 265-605) that associates with Cdc45, DNA polymerase epsilon, replication protein A, and two replication factor C complexes on chromatin [7].

References

Adaptation of a DNA replication checkpoint response depends upon inactivation of Claspin by the Polo-like kinase. Yoo, H.Y., Kumagai, A., Shevchenko, A., Shevchenko, A., Dunphy, W.G. Cell (2004) [Pubmed]
Site-specific phosphorylation of a checkpoint mediator protein controls its responses to different DNA structures. Yoo, H.Y., Jeong, S.Y., Dunphy, W.G. Genes Dev. (2006) [Pubmed]
Claspin, a Chk1-regulatory protein, monitors DNA replication on chromatin independently of RPA, ATR, and Rad17. Lee, J., Kumagai, A., Dunphy, W.G. Mol. Cell (2003) [Pubmed]
Claspin, a novel protein required for the activation of Chk1 during a DNA replication checkpoint response in Xenopus egg extracts. Kumagai, A., Dunphy, W.G. Mol. Cell (2000) [Pubmed]
Xenopus Drf1, a regulator of Cdc7, displays checkpoint-dependent accumulation on chromatin during an S-phase arrest. Yanow, S.K., Gold, D.A., Yoo, H.Y., Dunphy, W.G. J. Biol. Chem. (2003) [Pubmed]
Phosphorylation of Xenopus Rad1 and Hus1 defines a readout for ATR activation that is independent of Claspin and the Rad9 carboxy terminus. Lupardus, P.J., Cimprich, K.A. Mol. Biol. Cell (2006) [Pubmed]
Roles of replication fork-interacting and Chk1-activating domains from Claspin in a DNA replication checkpoint response. Lee, J., Gold, D.A., Shevchenko, A., Shevchenko, A., Dunphy, W.G. Mol. Biol. Cell (2005) [Pubmed]

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