Pubmed abstracts for Protein-Protein Interaction search result :


Interacting proteins: P22736 and P31749 Pubmed SVM Score :1.0380868
Thus , we show that Akt interacts with Nur 77 and inactivates Nur 77 by phosphorylation at Ser 350 in a phosphatidylinositol 3 kinase dependent manner , connecting the phosphatidylinositol 3 kinase dependent Akt pathway and a nuclear receptor pathway . . 1.0380868^^^
Interacting proteins: P22736 and P31749 Pubmed SVM Score :0.0
Predominant activation of IRS 2 was also observed in adult cardiomyocytes where HMR 1964 increased 3 O methylglucose transport and the activation of Akt and glycogen synthase kinase 3 to the same extent as human insulin . ^^^
Interacting proteins: P22736 and P31749 Pubmed SVM Score :0.0
We hypothesized that AMP activated protein kinase related kinase 5 ( ARK 5 ) / novel kinase family 1 ( NUAK 1 ) , an AMP activated protein kinase ( AMPK ) related kinase that has been found to be stimulated by protein kinase B ( Akt ) , would be expressed in rat skeletal muscle and activated by electrically elicited contractions , 5 aminoimidazole 4 carboxamide 1 beta d ribofuranoside ( AICAR ) , or insulin . ^^^
Interacting proteins: P22736 and P31749 Pubmed SVM Score :0.0
Nur77 / NGFI B , an orphan receptor superfamily transcription factor implicated in T cell apoptosis , is a substrate for Akt . ^^^ We hypothesized that TCL 1 transactivity is regulated through Akt induced phosphorylation of Nur77 / NGFI B in vivo . ^^^
Interacting proteins: P22736 and P31749 Pubmed SVM Score :0.0
Akt inhibits the orphan nuclear receptor Nur 77 and T cell apoptosis . ^^^ In this study , we demonstrate that one of the mechanisms by which Akt antagonizes apoptosis involves the inhibition of Nur 77 , a transcription factor implicated in T cell receptor mediated apoptosis . ^^^ It has been suggested that Akt phosphorylates Nur 77 directly , but whether Akt suppresses biological functions of Nur 77 remains unknown . ^^^ We found that Akt inhibited the DNA binding activity of Nur 77 and stimulated its association with 14 3 3 in a phosphorylation site dependent manner . ^^^ Moreover , we found that expression of Akt suppressed Nur 77 induced apoptosis in fibroblasts and activation induced cell death of T cell hybridomas . ^^^
Interacting proteins: P22736 and P31749 Pubmed SVM Score :0.0
Akt phosphorylates Nur 77 , thereby blocking its DNA binding ability and rendering the transcription factor inactive . ^^^
Interacting proteins: P22736 and P31749 Pubmed SVM Score :0.0
In the present study , we show that Nur 77 is phosphorylated on this site by RSK ( ribosomal S 6 kinase ) and MSK ( mitogen and stress activated kinase ) , but not by PKB ( protein kinase B ) or PKA ( protein kinase A ) , in vitro . ^^^
Interacting proteins: P22736 and P31749 Pubmed SVM Score :0.0
Regulation of Nur 77 nuclear export by c Jun N terminal kinase and Akt . ^^^ Induction of Nur 77 nuclear export by MEKK 1 required a prolonged MEKK 1 activation and was attenuated by Akt activation . ^^^ Expression of constitutively active Akt prevented MEKK 1 induced Nur 77 nuclear export . ^^^ Conversely , transfection of dominant negative Akt or treatment with a phosphatidylinositol 3 kinase ( PI 3 K ) inhibitor accelerated MEKK 1 induced Nur 77 nuclear export . ^^^ Furthermore , mutation of an Akt phosphorylation residue Ser 351 in Nur 77 abolished the effect of Akt or the PI 3 K inhibitor . ^^^
Interacting proteins: P22736 and P31749 Pubmed SVM Score :0.0
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