Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P67809 and P31749 Pubmed SVM Score :0.0
Elongation factor 1alpha ( EF1alpha ) and beta tubulin were identified as binding partners for the Akt 2 tail by peptide mass fingerprinting . ^^^ Using CHOT cells that overexpress insulin receptors and HA tagged Akt 2 , we showed that EF1alpha co immunoprecipitated with HA tagged Akt 2 . ^^^
Interacting proteins: P67809 and P31749 Pubmed SVM Score :0.0
In chicken embryo fibroblasts transformed by the oncoproteins P3k ( phosphatidylinositol 3 kinase ) or Akt , YB 1 is transcriptionally down regulated . ^^^ Expression of YB 1 from a retroviral vector induces a strong cellular resistance to transformation by P3k or Akt but does not affect sensitivity to transformation by other oncoproteins , such as Src , Jun , or Qin . ^^^ Both cap dependent and cap independent translation is inhibited in these cells , but the activity of Akt remains unaffected , suggesting that YB 1 functions downstream of Akt . ^^^ A YB 1 protein with a loss of function mutation in the RNA binding motif no longer binds to the mRNA cap structure , is localized in the cell nucleus , does not induce the flat cellular phenotype , and fails to interfere with P3k or Akt induced oncogenic transformation . ^^^
Interacting proteins: P67809 and P31749 Pubmed SVM Score :0.0
In this study , we determined that activated Akt is positively correlated with the protein expression of the transcription / translation factor Y box binding protein 1 ( YB 1 ) in primary breast cancer by screening tumor tissue microarrays . ^^^ We therefore questioned whether Akt and YB 1 might be functionally linked . ^^^ Herein , we illustrate that activated Akt binds to and phosphorylates the YB 1 cold shock domain at Ser 102 . ^^^ Following the stable expression of Flag : YB 1 and Flag : YB 1 ( Ala 102 ) in MCF 7 cells , we observed that disruption of the Akt phosphorylation site on YB 1 suppressed tumor cell growth in soft agar and in monolayer . ^^^ In conclusion , YB 1 is a new Akt substrate and disruption of this specific site inhibits tumor cell growth . . ^^^
Interacting proteins: P67809 and P31749 Pubmed SVM Score :0.0
Akt mediated YB 1 phosphorylation activates translation of silent mRNA species . ^^^ Here we demonstrate that association of YB 1 with the capped 5 ' terminus of the mRNA is regulated via phosphorylation by the serine / threonine protein kinase Akt . ^^^ We also show that similar to YB 1 , Akt is associated with inactive mRNPs and that activated Akt may relieve translational repression of the YB 1 bound mRNAs . ^^^ Using Affymetrix microarrays , we found that many of the YB 1 associated messages encode stress and growth related proteins , raising the intriguing possibility that Akt mediated YB 1 phosphorylation could , in part , increase production of proteins regulating cell proliferation , oncogenic transformation , and stress response . . ^^^
Interacting proteins: P67809 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P67809 and P31749 Pubmed SVM Score :0.0
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Interacting proteins: P67809 and P31749 Pubmed SVM Score :0.0
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