I'm running a high fever and I already reached the end of the internet. Time to go to MCP! Let's get this blog running again.
If you are a biologist, chances are you are familiar with p53 (shown in the image above that I brazenly stole from Dr. Andrew Martin's lab) That is because p53 is involved in all sorts of things. Primarily, however, it binds to DNA in response to damage and either stops or slows it's progression through the cell cycle. Many cancer cells are either deficient in p53 or have mutations in it or in proteins leading in its activation pathway somewhere.
The picture above (check out the link, it's cool) shows the frequency of mutations in p53, but that isn't what this article is about.
In press at MCP, is this very nice paper from Caroline deHart et al.,. In it they detail a high resolution proteomics approach to characterize the PTMs of p53 under different conditions.
On a technical level, they used p53 pull downs, ran them out on gels, and ran the gel fractions on an Orbi XL or Orbi Velos using either stage tips or an Advion NanoMate.
And they found PTMs all over the place. Phosphorylations, methylations, ubiquitin sites and on and on. This is a really cool paper to really illustrate how complementary genomic and proteomic techniques can be, because (as shown in the picture) we know an awful lot about the various mutations in p53, but that won't get us the whole story. Proteomics gets us another step closer.
Highly recommended for you cell cycle people (obviously) and my friends in the cancer realm.
Just a quick correction, this work is from the Perlman and Flint groups, both at Princeton University.
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