Protein SU
MOy
lation has been i
mp
licated in the pathogenesis of ische
mic stro
ke. However, the under
lying
mechanis
ms re
main unc
lear. Here, we found that g
loba
l brain ische
mia evo
kes a sustained e
levation of G
luK2 SUMOy
lation in the rat hippoca
mpa
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 sti
mu
lation. SUMOy
lation deficiency attenuated the
kainate-sti
mu
lated interaction between MLK3 and G
luK2. In addition, inhibition of
kainate-evo
ked 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 pro
motes its binding with MLK3, thereby activating the MLK3-JNK3 pathway, which
may be responsib
le for ische
mic neurona
l ce
ll death.
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