Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.60638944 |
The interaction of Cdk 4 with Cdc 37 in vitro was not sensitive to changes in ATP levels . 0.60638944^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
NA |
|
Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :1.1377575 |
Association of CDK 4 with both CDC 37 and HSP 90 may also imply a mechanistic link between the functions of CDC 37 and HSP90 . . 1.1377575^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.84859569 |
Cdc 37 competes with p 16 for binding to Cdk 4 , suggesting that p 16 might exert part of its inhibitory function by affecting the formation of Cdk4 / cyclin D 1 complexes via Cdc37 . . 0.84859569^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
In mouse fibroblasts , a primary target of Cdc 37 is Cdk 4 . ^^^ In insect cells , Cdc 37 is sufficient to target Hsp 90 to Cdk 4 and both in vitro and in vivo , Cdc37 / Hsp90 associates preferentially with the fraction of Cdk 4 not bound to D type cyclins . ^^^ Mammalian p50Cdc37 is a protein kinase targeting subunit of Hsp 90 that binds and stabilizes Cdk 4 . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
In cells expressing Cdk 4 only , growth is restored by overexpressing human Cdc 37 , a Cdk 4 binding molecular chaperone . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
The Cdc 37 gene encodes a 50 kDa protein which targets intrinsically unstable oncoprotein kinases such as Cdk 4 , Raf 1 , and src to the molecular chaperone Hsp 90 . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
CDC 37 encodes a 50 kDa protein that targets intrinsically unstable oncoprotein kinases including Cdk 4 , Raf 1 , and 5 src to the molecular chaperone Hsp 90 , an interaction that is thought to be important for the establishment of signaling pathways . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
With increased Cdc 37 expression , molecular analysis of Cdc 37 client pathways demonstrates enhanced Raf 1 activity , greater Cdk 4 levels , and reduced expression of the cyclin dependent kinase inhibitor p16 / CDKN2 . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
Crucially , the CK 2 phosphorylation of Cdc 37 on Ser 13 was essential for the optimal binding activity of Cdc 37 toward various kinases examined , including Raf 1 , Akt , Aurora B , Cdk 4 , Src , MOK , MAK , and MRK . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
Biochip analysis showed that SWCNTs can induce up regulation expression of cell cycle associated genes such as p 16 , bax , p 57 , hrk , cdc 42 and cdc 37 , down regulation expression of cell cycle genes such as cdk 2 , cdk 4 , cdk 6 and cyclin D 3 , and down regulation expression of signal transduction associated genes such as mad 2 , jak 1 , ttk , pcdha 9 and erk . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
This mutant can bind not only other Hsp 90 client protein kinases , Akt 1 , Aurora B and Cdk 4 , but also Cdc 2 and Cdk 2 , which to date have not been shown to physically interact with Cdc 37 . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
Consistent with similar work done with the cyclin dependent kinase relative Cdk 4 , the presence of the G box motif of Cdk 2 was shown to be critical for Cdc 37 binding , whereas consistent with work done with the Src family tyrosine kinase Lck , the presence of helix alphaC and the stabilization of helix alphaE were shown to be needed for Hsp 90 binding . . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
Upregulation of p 16 ( INK4A ) , Hsp 90 , and Cdc 37 genes ; an increase in Cdc 37 Cdk4 complexes ; and a decrease in p 16 ( INK4A ) Cdk 4 complexes occurred in preneoplastic liver , nodules , and hepatocellular carcinoma of F 344 rats . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
We present evidence indicating that phosphorylation of Cdc 37 by CK 2 in conserved Ser 13 in the N terminal extremity was prerequisite for the efficient binding activity of Cdc 37 to protein kinases including Akt , Cdk 4 , MOK , and Raf 1 . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
Chimeric mutants of Cdk 2 and Cdk 4 , which differ sharply in their affinities toward Cdc 37 , show that their C terminal portions may determine this difference . ^^^ |
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Interacting proteins: P11802 and Q16543 |
Pubmed |
SVM Score :0.0 |
Comparison with the crystal structure of Hsp 90 allows us to identify the locations of Cdc 37 and Cdk 4 in the complex and suggests a mechanism by which conformational changes in the kinase are coupled to the Hsp 90 ATPase cycle . . ^^^ |
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