@entity8498 initiates @entity5180 but not XXXX 3 kinase/ @entity584 , mediated signaling pathways in T lymphocytes.

@entity6370 @entity584 @entity6057 @entity5180 @entity10242 @entity563 @entity1889 @entity8498 @entity4357
@entity8498 is activated by the @entity6057 ( @entity6057 ) and then co-ordinates important signaling pathways for T lymphocyte activation. Effector pathways for this @entity6370 binding protein in T cells are mediated by the @entity563 / @entity1889 kinase @entity10242 and the Ras-related GTPase @entity5180 . In fibroblasts, an important effector for the Ras oncogene is @entity4357 3-kinase (PtdIns 3-kinase). Activation of this lipid kinase is able to induce critical @entity5180 signaling pathways and can couple @entity8498 to cell survival mechanisms via the @entity563 / @entity1889 kinase @entity584 . The role of PtdIns 3-kinase in Ras signaling in T cells has not been explored. In the present study, we examined the ability of PtdIns 3-kinase to initiate the @entity5180 signaling pathways important for T cell activation. We also examined the possibility that @entity584 is regulated by Ras signaling pathways in T lymphocytes. The results show that Ras can initiate a @entity5180 mediated pathway that regulates the transcriptional function of AP-1 complexes. @entity4357 3-kinase signals cannot mimic @entity8498 and induce the Rac mediated responses of AP-1 transcriptional activation. Moreover, neither @entity6057 or Ras activation of AP-1 is dependent on PtdIns 3-kinase. @entity584 is activated in response to triggering of the @entity6057 ; PtdIns 3-kinase activity is both required and sufficient for this @entity6057 response. In contrast, @entity8498 signals are unable to induce @entity584 activity in T cell nor is Ras function required for @entity584 activation in response to the @entity6057 . The present data thus highlight that PtdIns 3-kinase and @entity584 are not universal Ras effector molecules. Ras can initiate @entity5180 regulated signaling pathways in the context of @entity6057 function independently of PtdIns 3-kinase activity.
