Science Faculty Spotlight: Sebastien Poget

May 9, 2017

Sebastien Poget

Professor Sebastien Poget from the College of Staten Island’s Chemistry Department joined the Ph.D. Program in Biochemistry in 2009. He quickly become an integral part of the Program, participating in the mentoring of doctoral students and serving as a member of the Biochemistry Executive Committee and Admissions and Awards Committee. Below, we learn more about Dr. Poget’s background and current interests in biochemistry.

What is your academic background in biochemistry?

I started studying chemistry at the University of Basel because I was interested in dyes and inks, but as my studies progressed, I became more and more drawn to the chemistry of life, leading me to choose biology as my minor. Therefore, I started to look for a more biology-related place to do my Ph.D., settling in the end on the protein engineering group of Professor Alan Fersht at the University of Cambridge. This was a really fortunate choice as I was afforded the liberty of exploring many different angles to my project (structural and functional studies of C-type lectin domains) taking advantage of all the amazing expertise of different researchers in Alan’s vast group in the Department of Chemistry and the MRC Laboratory of Molecular Biology. With my interest in structural biology firmly established, I chose to focus my work on membrane transporters and channels through two postdocs in the groups of Dr. Roderick MacKinnon at Rockefeller University and Dr. Mark Girvin at Albert Einstein College of Medicine.

How did you become active in the Graduate Center Ph.D. Program in Biochemistry?

When I started my independent faculty position in the Department of Chemistry at the College of Staten Island, I joined both the Chemistry and Biochemistry Programs of the Graduate Center with the goal of recruiting Ph.D. students to pursue my research ideas. Biochemistry quickly became my primary home due to the fact that other students at our campus working in related areas at our campus (in the lab of Distinguished Professor Fred Naider) were all biochemistry students, as was my first recruit. In recruiting this student, I had experienced some of the problems that an outlying campus faces in attracting Ph.D. students. This showed me the importance of being actively involved in the graduate program, which I have been since 2011, when I was elected as our campus representative to the Biochemistry Executive Committee.

What is your current research, and how have students from the Graduate Center been involved?

My research focuses on questions of membrane protein structure and function in general, with our main focus currently on the interactions of animal peptide toxins with ion channel domains. We are working on elucidating the mechanism of action of such toxins (for example for a snake toxin with a highly unusual activating effect on the potassium channel KcsA) as well as on the discovery and characterization of new spider toxins that act on the voltage-sensing domains of sodium channels. My three biochemistry Ph.D. students, Mohammed Bhuiyan, Adel Hussein and Ryan Schroder, are all working in this area of research, learning how to make recombinant human sodium channel domains or fragments and using them for toxin discovery and structural studies of the toxin-channel interactions. Mohammed has just defended his thesis.

What is your greatest accomplishment since joining the CUNY faculty?

Together with my graduate student Mohammed Bhuiyan, we have succeeded in expressing, purifying and reconstituting one of the voltage sensor domains of the human cardiac sodium channel and using it for pull-down of new toxins. The cardiac sodium channel is of great medical importance since mutations in this gene are responsible for many fatal cardiac arrhythmias leading to sudden deaths from infants to adults. The ability to produce a functional domain of this very large and complex human protein opens the way for structural studies to investigate the consequences of these pathological mutations at the atomic level and to potentially design toxin-based or derived drugs to correct these malfunctions. We are currently pursuing this by continuing the identification and characterization of toxins acting on this channel domain and by optimizing our system for structural studies using NMR spectroscopy.

You are on sabbatical in Fall 2016 and Fall 2017; what projects are you doing during your sabbatical?

This semester, I am trying to spend some time in my own lab to wrap up the experiments for publishing some of our recent work, and am also spending time to write those papers as well as new grant applications. Furthermore, we are starting some collaborative projects, some of them involving faculty and the new facilities at the CUNY Advanced Science and Research Center (, and I expect to spend some part of my time there as well.

For next fall, I plan on expanding my research expertise to include expression of large eukaryotic membrane proteins in eukaryotic/mammalian expression systems and using cryo-electron microscopy for structurally elucidating these large and complex particles. This will allow us to look at the way in which toxins modify the gating properties of sodium channels at a global whole-channel level, which will provide a clearer picture of the overall mechanism in conjunction with the details that we are currently figuring out with our NMR studies of individual voltage-sensing domains.

What has been your most rewarding service you have provided as a Graduate Center faculty member?

The most rewarding aspect of being on the Biochemistry Executive Committee is definitely the interaction with the students, starting from the interviewing of prospective candidates to helping current students on our campus navigate the program, seeing their intellectual and personal growth and finally the culmination of a lot of hard work in the successful thesis defense.

Another rewarding aspect of being a part of the Biochemistry Program at the Graduate Center are the opportunities of interacting and getting to know colleagues throughout CUNY – it has truly been a privilege to be part of a program with colleagues that are not only excellent scientists but also highly supportive and collaborative in spirit.

What do you like to do in your free time?

Since I deal with the wonders of nature at the very small level in my work, I like to enjoy nature on a much bigger scale in my (unfortunately quite limited) free time, in particular by hiking and skiing in the mountains. I also coach my 9-year old son’s soccer team, a task for which I was even less prepared than for mentoring graduate students.

Text by the Ph.D. Program in Biochemistry