Certainly is, and as you might imagine phosphorylation of eIF-2α became a prime suspect as
a cause of the inhibition of translation initiation and, thereby, the
inhibition of protein synthesis after ischemia-reperfusion.
In the late 90s, work in our lab by Don DeGracia and others demonstrated that, in fact, eIF-2α is massively phosphorylated after an ischemic insult, to a degree sufficient to shut down all translation initiation in the neuron.
Caught in the Act. Here,
an antibody that recognized only eIF2α(P)--that is, only the
phosphorylated form if eIF2α, was used to "stain" brain sections from
rats. A. In the CA1 of a normal, nonischemic rat, very little staining
is seen, and that only in astrocytes (arrows). None is seen in CA1
neurons themselves. B. In the CA1 of an animal subjected to 10 min
global brain ischemia followe by just 10 minutes of reperfusion, it is
easy to see that the neurons have accumulated a ton of eIF2α(P). C. In
the cortex of animals subjected to the same insult as in B, the
pyramidal cortical neurons are full of eIF2α(P). D. By 60 minutes of
reperfusion, CA1 neurons begin to show eIF2α(P) in the nucleus.
Subsequent work by DeGracia and Sullivan mapped eIF-2α
phosphorylation to selectively vulnerable neurons. These
neurons, including the pyramidal neurons in CA1 hippocampus,
accumulated eIF-2α(P) quickly and never lost it. Resistant neurons also accumulated eIF-2α(P) during early reperfusion, but subsequently cleared it.