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Guest post by Chris Dieni

Happy New Year!

It’s often said that in order to move forward, you need to look back. We’ve just rung in a brand new year: 2011 has barely begun and yet, many of us are already booked to attend conferences, have deadlines to meet for grant applications, are scheduled to give departmental lectures, or have important meetings lined up for approving new patent proposals.

And already, we’re probably wondering what scientific discoveries or distinctions await us in 2011. We’ve had no shortage in the past few years! 2010 was all about “making” cells: whether it was the Nobel Prize in Physiology or Medicine being awarded for the development of in vitro fertilization, or a synthetic cell being created at the J. Craig Venter Institute. 2009 was a bit more subcellular: we focused more on enzymes like telomerase, and organelles like the ribosome, and it seemed—to me at least—like the word “epigenetics” had already become a household word. 2008, further back, was lit up by green fluorescent protein and what seemed like a long-overdue throwback to HIV. What wouldn’t 2011 conceivably hold in store for us?

For me, a biochemist who likes to think in molecular and mechanistic terms—perhaps even too much like a chemist at times (but don’t tell anyone)—2011 will probably focus on small chemical groups; that was also my focus of 2010, 2009, 2008 and essentially every year going back to 2004, at least! Because although I’m a biochemist—or as I like to professionally refer to myself, a comparative biochemist and physiologist—what I like to compare from enzyme to enzyme are the tiny little post-translational modifications that make a big difference in proteins. Up until late 2010, that was exclusively protein phosphorylation, but very recently I’ve branched into a bit of nitrosylation as well.

Many of us will look at phosphorylation and think “been there, done that.” British-born Canadian scientist Tony Pawson wrote about how phosphorylation had been around for 50 years—and that was already back in 2005! We know it’s true. A protein kinase puts on a phosphate group using ATP, and a protein phosphatase hydrolyzes it off. Those phosphates will change the kinetics of an enzyme, or the protein-protein interactions of a complex, or the activity of a receptor-bound signal transducer. It’s simple. And yet, it’s not. One of my personal highlights of 2010 was writing a five-part series for Bitesize Bio, a blog for biological scientists, about the Basics of Protein Phosphorylation. Writing those articles, picking apart the fundamental concepts of phosphorylation and detailing them in terms understandable to all, helped me to take a step back and look at a metabolic regulatory system that seems so complex, and yet so perfectly and elegantly orchestrated. In a way, given how smoothly the system runs—barring of course, the wide field of pathology—it’s understandable that it can be taken for granted; and yet, it’s a crime when it is.

A friend reminded me yesterday that 2011 is the International Year of Chemistry. This is something that I’ll be looking into and trying to participate in as much as possible. Because maybe—just maybe—it’s something that can get all of us
interested in the little guys again. Those phosphoryl, nitrosyl, acetyl, methyl, and other ornaments that decorate proteins like so much “bling” that the young people love these days; David’s biochemical slingshots to the Goliaths of synthetic cells and fertilized embryos that have been captivating everyone as of late.

So, will 2011 bring me some happiness, working on—and glorifying—these post-translational modifications that are so integral that, for the most part, they go unnoticed?

Absolutely! Want to jump on the bandwagon? There’s a lot of room.

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Chris is originally (and currently) from Montreal. After completing his bachelor’s degree, he made a short hop to the National Capital of Ottawa, Ontario. There, he worked on his Ph.D., studying extreme animals: freeze-tolerant frogs, hibernating ground squirrels, and the molecular mechanisms that allow them to survive. Chris then took a hike south of the Canada-USA border and did some postdoctoral research at Penn State. Carrying forward the phosphorylation momentum that he gained in grad school, he worked on signal transduction in the formation of protein complexes within HeLa cells. He is currently back in Montreal, working in the biotech industry. When not busy in the lab or at the desk, Chris enjoys watching (and ranting about) hockey, particularly the Montreal Canadiens and Ottawa Senators. He volunteers in mentoring programs for both his alma mater, and enjoys doing some scientific writing and blogging—especially for Bitesize Bio, for which he is a staff writer.

Edited to add: Tony Pawson is Head of our Cell Biology Faculty.