Protein SUMOy
lation has been imp
licated in the pathogenesis of ischemic stroke. However, the under
lying mechanisms remain unc
lear. Here, we found that g
loba
l brain ischemia evokes a sustained e
levation of G
luK2 SUMOy
lation in the rat hippocampa
l CA1 region. Over-expression of wi
ld-type G
luK2, but not SUMOy
lation-deficient mutant, significant
ly increased the activity of MLK3 and
JNK3 after kainate stimu
lation. SUMOy
lation deficiency attenuated the kainate-stimu
lated interaction between MLK3 and G
luK2. In addition, inhibition of kainate-evoked G
luK2 endocytosis decreased the activation of MLK3-JNK3 signa
ling and the binding of MLK3-G
luK2 in cu
ltured cortica
l neurons. These resu
lts suggest that the interna
lization of G
luK2 fo
llowing SUMO modification promotes its binding with MLK3, thereby activating the MLK3-JNK3 pathway, which may be responsib
le for ischemic neurona
l ce
ll death.
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