Heather Baker
Why did you decide to pursue a graduate degree?
I got involved with research pretty early and extensively in my undergraduate degree in biochemistry at the University of Alberta. The first research project I got to be part of was on developing a better cyan fluorescent protein. Although at the time I hardly knew anything about biochemistry, I was so excited to carry out the next experiment. This theme continued throughout my degree, and I found opportunities to work in several different labs. It was so rewarding to be part of different research projects and to push science forward in unique ways. I ended up doing my undergraduate honours thesis on a topic related to protein quality control in different cell types, which sparked my interest in the field and its implications in neurodegenerative disease. I knew I didn't want to stop my research career here - there was still so much I wanted to learn! Pursuing a PhD seemed like the next logical step, as I wanted to start to take ownership and drive my own project forward. I was able to find an awesome lab doing research on protein quality control at UBC that aligned with my research interests.
Why did you decide to study at UBC?
A big part of what brought me to UBC was the research. Professor Thibault Mayor’s research interests in proteostasis, aging, and using proteomics tools to explore these topics were what drew me to the idea of a PhD at UBC. The Department of Biochemistry and Molecular Biology (BMB) also seemed like such a supportive and productive environment for graduate students, with excellent and collaborative research taking place. The Mayor Lab is also part of the Michael Smith Laboratories, and I loved the idea of being part of an interdisciplinary research group. Finally, I loved the idea of living in Vancouver. It is such a beautiful, multicultural city. The proximity to the oceans, mountains, and lakes is unbeatable. It seemed like a no-brainer to not only have the opportunity to live in Vancouver but to carry out really cool research at an excellent university like UBC.
What is it specifically, that your program offers, that attracted you?
The research from the Mayor lab is what really attracted me to join BMB. However, once I visited for the interview day, I was able to fully appreciate how vibrant and diverse the research topics in the department are. In addition, there seemed to be many opportunities to network with visiting speakers, present my research to my peers, and participate in collaborative research projects which were definitely aspects I was interested in.
What was the best surprise about UBC or life in Vancouver?
The weather! As someone who was born and raised in Alberta, I was used to long and cold winters with lots of snow. While I knew that the Vancouver climate was much milder, not having to deal with snow every winter is still the best surprise.
What aspects of your life or career before now have best prepared you for your UBC graduate program?
Most directly would be my undergraduate degree from the University of Alberta. I am very grateful for the opportunities to get involved in research throughout my degree and for all the excellent mentors I had. While I learned a lot during my coursework, my mentors taught me a lot about science - whether that was the principles behind how a technique worked, how to be a better scientific writer, or how to ask the right research questions. These experiences have also taught me how to be a good mentor to other students, which in my opinion is one of the most important parts of graduate school.
What do you like to do for fun or relaxation?
Since moving to Vancouver, I’ve embraced the outdoors. In the summertime, I can be found hiking, camping, canoeing, paddle boarding, playing beach volleyball, and just generally trying to soak up the sun! In the winter, I try and hit the slopes as much as I can and am glad that I can still take advantage of student pricing at some of the local mountains! I also love that Vancouver has such a vibrant arts and culture scene, so I spend a lot of time at concerts, seeing stand-up comedy, and checking out local improv.
What advice do you have for new graduate students?
My first piece of advice would be to find a good work-life balance. While it can be easy to get caught up in the research (and sometimes the moment demands it), establishing hobbies and routines outside of school can help you feel grounded (and give you something to look forward to when that experiment fails!). My second piece of advice would be to celebrate your accomplishments regularly - no matter how small. I find that sometimes when things aren't working the way you want them to, or things take more time than you'd like, it's easy to be hard on yourself. It is also really easy to get caught up and compare yourself to others and feel what's known as "imposter syndrome". However, when you can look back and remind yourself of all the small and big wins, you can appreciate all the effort you've put in and how far you've come!
Outside of your academic work, what are the ways that you engage with your local or global community? Are there projects in particular that you are proud of?
In 2020, I joined the Department of Biochemistry and Molecular Biology's Equity, Diversity and Inclusion committee as a graduate student representative. Over the last three years on the BMB EDI committee, I’ve been very proud to be part of several different initiatives that our committee has been championing. My favourite would have to be starting up the BMB Mentorship Program. Together with a sub-group of graduate and undergraduate committee members, we initiated a BMB Mentorship Program to match BMB students and trainee mentors up with mentees. Having a strong role model and/or mentor that you can seek advice and guidance can be incredibly useful and can provide a sense of community for those in the BMB program. In particular, we wanted to give participants an option to connect with someone from a similar background, as underrepresented groups in STEM can often face different challenges, and meeting with someone who has shared similar experiences can be especially valuable. The program has received great feedback so far and I look forward to continuing this project.
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Learn more about Heather's research
Proteins are vital biological machines that ensure the survival of a cell. They participate in almost all crucial cellular functions, such as energy production, damage detection, and the facilitation of critical biological responses. The DNA that codes for these molecular machines, however, can often be mutated. Genetic mutations, such as those in genetic diseases, can lead to improper protein folding which can result in a loss of function or unwanted interference with other cellular processes. Improper protein folding and aggregation is also a hallmark of neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's disease. To recognize and respond to these potential obstacles, our cells have evolved to employ a sophisticated quality control network. Chaperones, a type of protein that assists others in folding, are typically thought of as the first line of defence during protein misfolding. However, when a protein is unable to refold into its native state, chaperones and other co-factors work in concert with the ubiquitin proteasome system (UPS) to modify aberrant proteins with a unique tag, known as ubiquitin, so they can be degraded. Existing research suggests that protein quality control is compartmentalized within the cell. While this process is well understood in certain organelles, the underlying recognition, tagging, and triaging of proteins that misfold in the cytosol remains underexplored. This is particularly important because many proteins, including those that are mutated in rare genetic diseases, are translated and function within this cellular space. My research interest is to better understand the mechanisms by which these cytosolic misfolded proteins are recognized by the cell to be degraded. In particular, I want to determine if there is a key E3 ligase enzyme that can recognize a broad array of cytosolic misfolded proteins or whether some cytosolic misfolded proteins share a common recognition motif. E3 ligases are enzymes that can recognize aberrant proteins and decorate them with ubiquitin. However, there are over 600 mammalian E3 ligases and how many of them can select their protein targets is not well characterized. Additionally, I am interested in the role of chaperones and other auxiliary proteins when a cytosolic protein misfolds. This project aims to understand which players are key to the destruction of errant proteins, how they triage damaged proteins and how this can be applied to new treatments for rare diseases.