Receptor-interacting protein 3 (RIP3) has been implicated in ischemic necrosis of retinal cells. An
in silico analysis followed by experimental validation identified death associated protein (
Daxx) as a novel substrate of RIP3.
In vitro binding studies revealed that RIP3 binds to the serine/proline/threonine-rich domain (amino acid 625-740) of Daxx. Upon ischemic insult, RIP3 phosphorylated Daxx at Ser-668 in the retinal ganglion cells, triggering nuclear export of Daxx. Depletion of RIP3 significantly inhibited nuclear export of Daxx and attenuated cell death to a great extent. Collectively, the findings of this study demonstrate that phosphorylation of Daxx by RIP3 comprises an important part of ischemic necrosis in rat retinal ganglion cells.
Structured summary of protein interactions
to by down (View Interaction: , ) and by microscopy () with by () to by()
