Lysine acetylation is another of the myriad levels of controls our bodies use to regulate lots of things -- possibly everything! who knows at this point?!?! What we do know is that it is there and we can find a few of this mod in almost any global proteomics experiment if we look for it. What we haven't had is a streamlined workflow for going after these modifications to find what, if any, patterns exist in different states.
Tanya Svinkina et al., (in press at MCP and currently open access here!) have now changed that (BOOM!)
In this study, this group uses a mixture of commercially available antibodies (that you can buy right now, if you want) to selectively enrich peptides with lysine acetylation. They perform this enrichment on multiple cell lines and throw in both SILAC and reporter ion quantification reagents along the way just for kicks.
As I said, we have some idea of what this mechanism does and since a lot of these researchers are affiliated with the Broad (like toad!) they apply it to a bunch of different cell lines including mouse, and human cancer cells. By the way, that GIF above is really distracting while typing....
LC-MS analysis of the samples was performed with either an Obitrap Elite or Q Exactive.
How'd it turn out? For one, they ended up with more lysine acetylated peptides than anyone has ever reported getting at once. For two(?), they showed that their relatively simple technique for enrichments and LC-MS analysis was easily applicable to SILAC, iTRAQ, and TMT. For three(??) they found that about 50% of lysine acetylation sites were conserved between the mouse and Jurkat cancer cell lines (woo!). Anything that is that conserved amongst species is super important, suggesting that further analysis of this PTM is pretty critical to our fundamental understanding of mammalian biology.
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