Hughes Mentor:  Richard Cerione

Department: Vet Molecular Medicine

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An Interview with Dr. Richard A. Cerione

∑ Where did you go for Undergraduate and Graduate school?
- Rutgers

∑ What made you decide to come to Cornell?
- Basically, you go through a process: you get a PhD, become a post doc... Etc...
To summarize- I was finishing my PhD at Rutgers. I then went to Duke. A faculty position opened at Cornell and so I took the job.

∑ At what point did you choose this career? What influenced you to choose this career?
-I chose it late in my life. I started off as an engineer. Some reason I found it boring. Suring grad school, my friends and roommates were Medical students. I picked up Biochemistry and found a newfound love for it. I therefore switched from doing my Chemical Engineering major to do a Biochemistry major. They were similar majors; I just had to take extra subjects like Biology for example. But once I finished the course, I didn’t know what to do next, you know? By the time the summer after grad school, I still had no plans. I hadn’t even done my GREs. Rutgers took me in without a GRE. So it was a last minute decision. But the fantastic thing is, once I started, I KNEW this was it. This was what I wanted to do. I loved it.
∑ Do you have any mentors? Who do you idealize?
- There were many people who helped me along the way. Especially Efrain Racker, he’s a famous biochemist at Cornell in Bioenergetics. I followed his work in cancer. I liked the way he thought. I liked his thinking. We had lunch together many many times. We spoke about research and many other things. Great guy.
∑ What was the appeal of this job?
- Why research. Like I said before, I never realized at first I wanted to do something in science. I remember in junior high school, specifically in 7th grade. I learned about DNA. As my teacher explained what DNA was, I was captivated. The idea of DNA encoding everything was amazing. I loved it. I still remember that day. I’ve learned about rocks, physics- but nope nothing had interested me as much before. Years later, that interest sprung back. I loved the way research work is like detective work. Solving all these mysteries- mysteries of how things work and what happens in certain conditions-its intriguing. I also liked the lab atmosphere with all the students and post-docs. The students come in inexperienced and walk out very experienced. I’ve never regretted its challenges: keeping the lab funded, helping the students (both graduate and undergraduates) grow. Research is a wonderful combination of many aspects.

∑ How successful has your PhD been? How do you define success?
- Well, there are the obvious ones, for example: the number of papers you have, number of funding, and amount of funding. These, in my opinion are not good indications of success. See nowadays, students come into relatively rich labs. Back in the day, we weren’t in rich labs. The guy who ran my lab loved it. He gave me a chance to fall in love with science even when there weren’t many facilities. I grew up falling in love with my work. I love doing this. It’s not only about the ‘obvious things’. It’s about finding and getting into the career that you love. It’s about loving your work. I was lucky enough to find mine. That’s success in my book. I found something wanna wake up and do. Success is doing what you love.

∑ What do you do for fun when you aren’t doing research?
-No fun for me…hahahah. Well, I have two kids. I love balancing family with my career. I do the best I can. I am also passionately in love with the NFL Philadelphia Eagles. I try to watch games every Sunday.

∑ What do you look for in undergraduate researchers?
- We don’t take a lot of undergrads. We take more PhDs in our lab. We usually hope to find someone who is very interested. Some people are there just to fulfill requirements- they really don’t care. I’m not upset with them. Their just doing what they have to do to get where they want to go. But some people have a spark. They are curious and you can see it. So we try to get people who are genuinely interested, but the problem is you will not know if they are or aren’t until they have been in lab for a while.

∑ What specific goals have you established for your career?
- I hate goals… and policies… and rules. We get funding from NIH- they want us to have goals and hypothesizes. So we do. But I like the unknown. I like not knowing what I’ll stumble across. It’s exciting.

∑ What do you think it takes to be successful in this career?
-Perseverance , Curiosity, Involvement

∑ What quality or attribute do you feel will most contribute to your career success?
- Just getting lucky. Getting into something you like.

Writing Assignment: A day in the life of an undergraduate in the Cerione lab

My morning routine starts with a little breakfast at home, followed by my daily walk from my home in Collegetown to the Veterinary College out on East campus. While it’s a bit of a hike, it’s a good a way as any to wake up. I generally arrive around 9:30, and get moving pretty quickly on whatever the day’s project is. I’m admittedly not much of a morning person, but after shifting my schedule back a few hours (and consequently having to stay at lab until 8-9pm for a few days), I see the value in getting started at a rational time. I’m lucky in that I really like the project I’m on - there’s always a reason to hop into lab, even if I’m a bit groggy.

I joined the Cerione group during the second semester of my sophomore year (although I didn’t start until that summer). During that year, I had worked at the Lab of Ornithology and discovered my dissatisfaction with both organismal biology and population genetics, while at the same time massively enjoying my courses in organic chemistry. The final straw was being told by my mentor at the Lab of O. that my lab skills weren’t up to snuff and that I should try out a computer-based project. I hate programming, so during the latter half of the spring semester I began looking for a lab in which to do biochemistry-oriented research. Initially, I was really interested in working in the Baird group (and even attended a few group meetings), but was finally told that there just wasn’t room at the time. Dr. Baird, however, did recommend that I check out the Cerione group, and in short order I had set up an interview (with a little help from my organic chem. professor, Tom Ruttledge, who provided an excellent rec. letter). After a brief talk with Rick himself, I met with my mentor, Marc, and discussed the project I’d be working on - figuring out the interactions of an interesting enzyme related to cancer cell nastiness called tissue transglutaminase with other proteins - essentially, I’d working on filling in a “black box” of a cellular signaling pathway. I’ve been on the same project since then, and still find it an engaging and challenging topic of study. I’m attracted to studying proteins for a few reasons, but primarily because they are the “machines” of the cell - whereas genes encoded in DNA is a script, proteins are actors.

Working with proteins as I do, one technique is central - Western blotting. Basically, with a WB, you load denatured samples of proteins (denaturing linearizes the molecules, a detergent in the sample buffer also loads up the molecules with negative charges) into the wells of a gel, then apply an electric field. This separates the proteins by molecular size. Once the gel is run, you can transfer the proteins to a membrane, and from there, identify and image specific protein “bands” with specific antibodies conjugated to a light-emitting enzyme (horseradish peroxidase) - and finally, the blot can be imaged in a darkroom with x-ray film. Blots are the read-outs for nearly all my experiments, be they with cell lysates or be they in-vitro, pure protein-protein interaction assays - each well and gel lane represents a different set of chemical conditions. Culturing cells - and keeping them fed and happy - is important too. While I think “wet lab” molecular biology has a bit of a learning curve, this summer in particular has been really productive, since I’ve mastered nearly all the techniques I use. No longer do I forget to, say, wash a blot and wind up staring at a black featureless square after developing the picture!

I’m definitely indebted to my mentor’s incredible patience.

Anybody who does molecular biology knows that in practice, there’s a good deal of downtime. In between incubations, I frequently read - sometimes current papers in my field, though just as frequently I can be found with a GRE book. If some process is particularly long - say, two or three hours, I might take a walk - and perhaps get some ice cream at the conveniently located Dairy Bar…

As summer ends, I’m looking forward to the new routines involved with taking a full course load - and I certainly don’t put my research on hold. As I did last year, I’ll continue going into lab daily - the trick is to take mostly morning classes, and be in lab by noon or so. Balance is definitely possible if you use your downtime properly - studying is the best use.

I’ve been really lucky to work with the people in the Cerione group, and to have a project I enjoy pursuing. I plan on continuing to do research here throughout the last two semesters of my time at Cornell - I’m just too interested and in too deep to do anything else!

A Hughes Scholar Guide to Doing Research in the Cerione Lab

Before you actually begin research in a laboratory, it’s a good idea to do a little exploring. It’s important to find out what fields you are genuinely interested in because much of your free time after joining a lab will be spent on your independent project. You wouldn’t want to be stuck doing daily PCR’s if where you really want to be is out in the field collecting avian tissue samples.

This is how my first foray into research began. I consulted every available resource in the Office of Undergraduate Biology (OUB), including the Head of Undergraduate Research, Laurel Southard. After I explained that my research interests paralleled my Program of Study, Molecular and Cell Biology, she advised me to e-mail Professor Richard Cerione of the Department of Molecular Medicine. I did and set up an interview with the Senior Research Associate of the lab in charge of undergraduates, Dr. Jon Erickson.

I had always worried that my somewhat generic science background would prevent me from finding placement in a lab (I had only taken a few of the biology major’s requirements including general biology, chemistry, physics, and organic chemistry). However, Dr. Erickson assured me that much of my education would be hands-on. I would learn the necessary techniques not only from reading manuals and papers, but also by performing the actual experiments.

The Cerione group’s research revolves around the visual pathway of vertebrates (Fig. 1). While certain members of the lab endeavor to solve the crystal structures of the pathway’s proteins, others perform mutational analysis of highly conserved amino acids. My project revolves around the latter. Specifically, it focuses on the protein, transducin, and how certain amino acids contribute to its overall activation.

When I was first starting out, a typical day began with Polymerase Chain Reactions (PCR) to obtain the plasmid DNA that coded for my mutated protein of interest. Three and a half hours later, these PCR products would be inserted into plasmid vectors that would be used to transform E. coli cells. Sometimes the efficiency of this process left much to be desired and it could take anywhere from one day to a few months to get a successful transformation. However, if the stars were aligned and the gods were appeased, my transformation worked, allowing me to move on with my project to protein expression, purification, assays.

One of the best tests to determine the activity of a protein construct is to see if it can bind its corresponding ligand. In the case of transducin, it normally binds guanine nucleotides (GTP, GDP). Thus, my very first assay was a radioactive binding assay in which nucleotides were radioactively labeled with 35S and incubated with both wild type and mutant proteins. The amount of radioactivity detected in the sample would be proportional to the amount of nucleotide successfully bound by the construct. By comparing results between wild type and mutant, I was able to answer some of my project’s questions. For example, “If I mutate a negatively charged glutamic acid into a positively charged lysine, would it disrupt the active structure of transducin?”

This past year has been a rigorous educational experience. Not only did I have to contend with upper level courses as a junior, but I also needed to improve upon my time management skills. Doing research while taking classes is a constant juggling process in which one’s priorities switch from day to day. For instance, sometimes I went into lab even though I had a prelim that same night. During other days, I needed the extra time to prepare for exams and simply went home to study knowing that I would have to make up for lost time the following day. If I learned anything from two summers and two semesters of research, it’s this: don’t slack off during the summer. If you get the chance to stay at Cornell during the “off-season,” make the most of it because it’s your best chance to make significant progress.