Pubmed abstracts for Protein-Protein Interaction search result :

Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
CK 2 cooperates in transforming cells with other lymphoid oncogenes such as myc and tal 1 , and here we show cooperativity with loss of the tumor suppressor gene p 53 . ^^^
Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
Functional interaction of protein kinase CK 2 and c Myc in lymphomagenesis . ^^^ Since c myc can be phosphorylated by CK 2 , we hypothesized that the synergy between CK 2 and c myc might be due to a functional interaction of the two molecules . ^^^ Pharmacologic inhibition of CK 2 activity in cell lines established from CK2alpha transgenic T cell lymphomas reduces their proliferation and concomitantly with this , the steady state levels of c myc protein decline . ^^^ Transfection of cells with sense or anti sense CK 2 constructs modulates c myc protein levels in concert with the alteration in CK 2 activity , validating the findings obtained using the kinase inhibitors . ^^^ Thus , CK 2 is a critical regulator of c myc protein stability and of the proliferation of these T cell lymphomas . . ^^^
Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
Activation of casein kinase 2 ( CK 2 ) was one of the first observations made on how Theileria parasites manipulate host cell signal transduction pathways and we argue that CK 2 induction may in fact contribute to many of the different activation events that have been described since 1993 for Theileria infected lymphocytes such as sustained activation of transcription factors c Myc and NF kappaB . ^^^
Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
In contrast , phosphorylation of Max and / or Myc by CKII had no inhibitory or stimulatory effect on the DNA binding activity of Myc / Max heterodimers . ^^^
Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
Myc proteins are phosphorylated within two critical regions by casein kinase 2 ( CKII ) : the central acidic domain and a carboxy terminal region bordering the basic region helix loop helix segment . ^^^ The Myc CKII site mutants were cloned into a retroviral vector and were shown to be efficiently expressed in several different cell types . ^^^ While the CKII site is non functional in this assay , the high levels of Myc produced may have overridden potential CKII regulation . . ^^^
Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
We have identified CKII phosphorylation sites in c Myc , Max , and c Myb which are phosphorylated in the cell . ^^^ Whereas little evidence to any functional significance of the CKII sites in c Myc has been obtained , phosphorylation of its heterodimeric partner Max alters DNA binding properties . ^^^
Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
Both Myc Max and Mad Max heterocomplexes are favored over Max homodimers , and , unlike Max homodimers , the DNA binding activity of the heterodimers is unaffected by CKII phosphorylation . ^^^
Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
Since a number of potential nuclear CK 2 targets have been reported , including the oncoprotein myc , it is suggested that the nuclear translocation of the kinase as characterized in vitro may have a biological significance in living cell , especially in the control of nuclear activities related to cell proliferation and the mechanism of action of growth factors . . ^^^
Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
Polyamines , casein kinase 2 ( CKII ) , and the myc oncogene are directly involved in the regulation of molecular events in cell proliferation , differentiation , and apoptosis . ^^^ In our current study , we showed that the Km values for purified CKII were similar for casein and Myc oncoprotein under a variety of assay conditions , and that specific natural and synthetic polyamines stimulated CKII phosphorylation of Myc oncoprotein 2 to 20 fold via increases in Vmax . ^^^ Because the Myc oncoprotein transactivates several genes for key proteins involved in the regulation of cellular proliferation , including the omithine decarboxylase gene ( rate limiting enzyme of polyamine synthesis ) , we suggest that there may be linkages between polyamines , CKII , and Myc in the control of cellular proliferation . ^^^
Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
Phosphorylation of MAZ by CKII at this serine residue was required for maximum binding of MAZ to the pyrimidine rich DNA of the nuclease hypersensitive element ( NHE ) in the 5 ' end promoter region of the c myc gene . ^^^ Moreover , the mutated MAZ was unable to enhance the expression of luciferase encoded by a c myc promoter / luciferase reporter gene in HeLa cells in the presence of CKII . ^^^
Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
From these data , it can be concluded that ( 1 ) the stimulation of CKII by prolactin in Nb 2 cells is concomitant with cell multiplication : ( 2 ) MAPK stimulation is not necessary for prolactin to induce Nb 2 cell multiplication ; and ( 3 ) PKC is stimulated in mammary and Nb 2 cells , but this stimulation is not required for prolactin to stimulate casein , c myc , beta actin and stathmin gene expression and Nb 2 cell division . . ^^^
Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
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Interacting proteins: P68400 and P01106	Pubmed	SVM Score :0.0
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