Caspases are proteins that chew things up. If you didn't know better, they look like they chew things up completely indiscriminately -- every protein gets chopped up. This is really useful for controlling diseased cells during things like apoptosis. This cell is bad, program cell death, destroy everything.
This awesome new paper in this month's MCP from Jacob Turowec et al., (permanently open access!) shows that caspase cleavage may not be indiscriminate at all. In fact, it may be regulated, while it is happening, by protein phosphorylation.
To decipher this, the team employed an unbiased n-terminal approach they call TAILS and analyzed the rate of degradation of proteins in caspase activated systems. The analysis was performed on an Orbitrap Velos and the data was analyzed with MaxQuant.
They find that some phosphorylation events lead to increased cleavage rates and some lead to decreased rates. Interesting, right! It seemed strange that we would just auto-self destruct cells indiscriminately. Even in this worst case scenario, it appears that we have some measure of control after all.
I stole this image from their paper because its cool and describes their aproach.
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