| Interacting proteins: P30307 and P27448 |
Pubmed |
SVM Score :0.67272051 |
| Taken together , these results suggest that one function of C TAK 1 may be to regulate the interactions between Cdc25C and 14 3 3 in vivo by phosphorylating Cdc25C on serine 216 . . 0.67272051^^^ In addition , a physical interaction between C TAK 1 and Cdc25C was observed upon transient overexpression in COS 7 cells . 0.5606355^^^ |
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| Interacting proteins: P30307 and P27448 |
Pubmed |
SVM Score :0.0 |
| Here we show that the protein kinase Cdc 25 C associated kinase 1 ( C TAK 1 ) is a binding partner and a substrate of Pim 1 . ^^^ |
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| Interacting proteins: P30307 and P27448 |
Pubmed |
SVM Score :0.0 |
| Of the three kinases known to phosphorylate Cdc25C on Ser 216 , both checkpoint kinase 1 ( hChk 1 ) and Cdc25C associated protein kinase 1 ( cTAK 1 ) were potently inhibited by UCN 01 with IC50s of 11 and 27 nM , respectively . ^^^ These results suggest that disruption of the DNA damage induced G 2 checkpoint by UCN 01 is mediated through the inhibition of the Cdc25C kinases , hChk 1 and cTAK 1 , and that hChk 2 activity is not sufficient to enforce the G 2 checkpoint in cells treated with a pharmacological inhibitor of hChk1 . . ^^^ |
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| Interacting proteins: P30307 and P27448 |
Pubmed |
SVM Score :0.0 |
| UCN 01 inhibits Chk1 / 2 , which should activate the mitosis inducing phosphatase Cdc25C , yet this phosphatase remained inactive during S phase progression induced by low concentrations of UCN 01 , probably because Cdc25C is also inhibited by the constitutive kinase , C TAK 1 . ^^^ High concentrations of UCN 01 caused rapid activation of Cdc25C , which is attributed to inhibition of C TAK 1 , as well as Chk1 / 2 . ^^^ |
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| Interacting proteins: P30307 and P27448 |
Pubmed |
SVM Score :0.0 |
| Cdc25C associated kinase 1 ( C TAK 1 ) has been implicated in cell cycle regulation and Ras signaling through its interactions with two putative substrates , the Cdc25C phosphatase and the MAPK scaffold KSR 1 . ^^^ Using a mutational approach to disrupt binding of C TAK 1 to KSR 1 and Cdc25C , we demonstrate that C TAK 1 contributes to the regulation of these proteins in vivo through the generation of 14 3 3 binding sites . ^^^ Disruption of the Cdc25C C TAK 1 interaction resulted in reduced 14 3 3 binding site phosphorylation and nuclear accumulation of Cdc25C in interphase cells . ^^^ |
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| Interacting proteins: P30307 and P27448 |
Pubmed |
SVM Score :0.0 |
| Cdc25C is functionally related to Cdc25A but acts specifically at the G2 / M cell cycle transition point and can be inactivated by C TAK 1 mediated phosphorylation . ^^^ |
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