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- 2024
- Scientists develop tool to predict sepsis in apparently healthy newborns
- Dr. Lynne Quarmby, cool new discoveries about Watermelon Snow
- Dr. Valentin Jaumouillé and Dr. Amy Lee, Molecular Biology and Biochemistry researchers receive Michael Smith Health Research BC Scholar awards
- Dr. Ryan Morin has been honored with the Bernard and Francine Dorval Prize from the Canadian Cancer Society
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- Royal Society of Canada bestows Dr. Vocadlo with country’s highest academic honour
- Decoding the genome to predict the clinical course of lymphomas
- 2023 Award for Excellence in Supervision: Esther Verheyen
- In a recent Nature Communications paper, the Audas lab demonstrates that proteins can act as microscopic thermometers to sense and respond to changing environmental conditions
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- Science Advances paper by new MBB PhD, Casey Engstrom and Professor Lynne Quarmby uses satellites to study the impact of Watermelon Snow on glacier loss in North America
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Audas Lab
Understanding the role of noncoding RNA in the reversible formation of amyloid aggregates.
Noncoding RNAs (ncRNAs) have recently emerged as important regulators of essential cellular pathways. These molecules possess remarkable functional divergence, acting as transcription/translation factors, epigenetic regulators and architectural molecules. In general, ncRNAs are thought to “fine-tune” the basic proteomic machinery and enhance cellular adaptability in response to environmental stressors. Regardless of the stimulus (e.g. heat shock, metabolic deprivation or DNA damage), many ncRNAs facilitate a state of proliferative arrest, allowing the cell to focus its resources on pathways critical to its survival. As the list of functional RNA molecules continues to rapidly expand, it is becoming increasingly clear that the significance and functionality of this family of transcripts may someday rival that of proteins.
Our research group studies a newly discovered extracellular stress-response pathway, whereby ncRNAs regulate the rapid and reversible conversion of proteins into amyloid-like structures. Remarkably, these natural amyloids possess most of the biochemical properties associated with the plaques and aggregates observed in Alzheimer’s, Parkinson’s and prion-based diseases, suggesting that dysregulation of this biological pathway could be a common cause of many neurodegenerative disorders. We are focused on identifying the environmental and cellular factors that mediate the formation and disassembly of these natural amyloid aggregates, while considering the translational significance of this work to prevent and treat neurological diseases.
For more details, visit our lab website.
Selected Publications
- Marijan D, Momchilova EZ, Burns D, Chandhok S, Zapf R, Wille H, Potoyan DA, Audas TE (2024). Protein thermal sensing regulates physiological amyloid aggregation. Nature Communications. 15 (1): 1222.
- Chandhok S, Pereira L, Momchilova EA, Marijan D, Zapf R, Lacroix E, Kaur A, Keymanesh S, Krieger C, Audas TE (2023). Stress-mediated aggregation of disease-associated proteins in amyloid bodies. Scientific Reports. 13 (1): 14471.
- Lacroix E, Pereira L, Yoo B, Coyle KM, Chandhok S, Zapf R, Marijan D, Morin RD, Vlachos S, Harden N, Audas TE (2021). Evolutionary conservation of systemic and reversible amyloid aggregation. Journal of Cell Science. 134 (22): jcs258907.
- Audas TE et al. (2016). Adaptation to Stressors by Systemic Protein Amyloidogenesis. Developmental Cell. 39(2):155-168.