@entity563 - XXXX kinase 38 is regulated by glycogen synthase kinase-3 and modulates oxidative stress-induced cell death.

@entity8785 @entity274 @entity563 @entity30092 @entity2307 @entity584 @entity493 @entity6709 @entity1889 @entity49166 @entity9459 @entity4357
@entity563 - @entity1889 kinase 38 ( @entity30092 ) is a member of the protein kinase A (PKA)/ @entity6709 /PKC-like family. In the present study, we investigated the regulatory mechanism of @entity30092 and assessed its role in the cellular stress response. Among various environmental stresses, @entity30092 was specifically activated by @entity274 , and the @entity4357 3-kinase inhibitor @entity2307 or @entity584 inhibitor IV suppressed this activation. @entity30092 was also activated by a constitutively active @entity584 or by @entity9459 inhibitor VII. The phosphorylation level of @entity9459 was correlated with the @entity30092 activity, in response to various stimuli and in different cell lines. Co-immunoprecipitation analysis revealed that @entity9459 physically interacted with @entity30092 in cells. @entity9459 overexpression inhibited the @entity274 -stimulated @entity30092 activity. @entity9459 phosphorylated @entity30092 on residues S6 and T7 in vitro, depending largely on a PKA-mediated priming phosphorylation of @entity30092 on residues @entity8785 and @entity49166 , respectively. @entity30092 's @entity274 -stimulated activity was enhanced by @entity493 substitution at its priming sites and/or at S6 and T7, and it was partially reduced by a phosphomimetic mutation at S6 or T7. @entity30092 knockdown enhanced the @entity274 -induced JNK phosphorylation and cell death. Our results indicate that that @entity9459 inhibits @entity30092 's full activation, and suggest that @entity30092 activation is required to prevent cell death in response to oxidative stress.
