SUMOylation is a PTM that I generally try to forget about, because
1) I don't know how to identify it and
2) I don't know what it does, except...well...if it messes up it's probably bad.
Solution? This great new paper in Press at MCP!
SUMOylation is a protein-type PTM -- something like ubiquitination, but without the handy-dandy lysine on the third amino acid post-protein binding. We'll probably find out tomorrow, if we haven't already, that this isn't true -- but, ubiquitination means DESTROY THIS PROTEIN IMMEDIATELY. SUMOylation on a protein -- well...I don't think we're entirely sure, but if the last couple amino acids aren't cleaved off, it doesn't do anything.
This study solves problem #1 for me. These authors describe an enrichment procedure for SUMOylation that they can control in fine detail using Flag tags and stuff. Even better? They develop a protein microarray for SUMOylation substrates! YES.
Potential collaborators of the future, "What about SUMOylation?"
Ben, "Great idea! Here are the names of 18 people in beautiful Baltimore who know how to do this with protein microarrays. I even know a couple of them. Let's go visit and get a Natty Boh, hon!"
Hey, if you can monitor a variable and complicated PTM with an array. I say do it with an array. And if you aren't interested in sites or are doing exploration, this great paper walks you through the molecular techniques to get a global picture of this weird and complicated modification.