|Academic Profile |
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Asst Prof Guillaume Thibault
Assistant Professor, School of Biological Sciences
|Guillaume Thibault PhD specialized in molecular chaperones in protein folding and degradation and on cellular stress responses and homeostasis. Notably, he designed unique strategies to reveal new roles of the unfolded protein response (UPR) in proteotoxic and lipid bilayer stresses. In his lab, he combines his multidisciplinary training to tackle biological key questions on ER stress, lipid regulation, and homeostasis using model organisms yeast, cell culture, and C. elegans. He was awarded the highly competitive Elite Nanyang Assistant Professorship Award 2013.|
2013 Post-doctoral Research Fellow, Temasek Life Sciences Laboratory, National University of Singapore
2007 Ph.D. in Biochemistry, University of Toronto, Canada
2002 B.Sc. in Biochemistry, Université du Québec à Montréal, Canada
1999 Diploma in Analytical Chemistry, Collège Ahuntsic, Canada
|LIPID REGULATION IN EUKARYOTES|
Hundreds of distinct lipids, of varying concentrations, assemble to form biological membranes. The most abundant, phospholipids, varies according to head group structures, acyl chain length and double bounds. In eukaryotes, lipid compositions can differ widely among organelles. In most cases, the biological significance of these differences remains unclear
The complex organization of cellular membranes suggests the need of sophisticated homeostatic regulatory mechanisms. Links were made with an endoplasmic reticulum (ER) stress pathway called the unfolded protein response (UPR). The UPR activation is required to ease the damaging effects of ER stress. Yeast relies exclusively on the Ire1p pathway while metazoans have two additional UPR outputs. This characteristic makes budding yeast a very attractive model organism since its sole UPR pathway can be easily manipulated. Normally, this response leads to ER homeostasis by facilitating refolding of proteins and enhancing recognition and degradation of misfolded proteins. Meant to be temporary, the UPR must be deactivated to avoid cell death due to chronic ER stress. Many diseases, such as Alzheimer, Parkinson, diabetes mellitus type 2, and hepatic steatosis, have been linked to recurrent ER stress.
- Catalytic synthesis and metabolism of site-specific deuterated essential fatty acids
- Characterising the anti-aging role of the UPR from high glucose diet
- Dissecting the neuroprotective role of WDFY3 to counteract age-mediated decline in proteostasis.
- Elucidating exosomes biogenesis and uptake in cancer progression
- From Dietary Excess to Neurodegeneration: Finding the Missing Links in Vesicular Autophagic Transport, Degradation, and Stress
- Identify Essential Genes to Construct A Functional Unfolded Protein Response Programme Using Synthetic Biology
- Improving student learning using open-ended question assessment with machine learning-driven immediate feedback
- LKCMedicine Internal Grant 25
- Xiu Hui Fun and Guillaume Thibault. (2020). Lipid bilayer stress and proteotoxic stress-induced unfolded protein response deploy divergent transcriptional and non-transcriptional programmes. Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids, 1865(1).
- W.W.B. Goh, S. Thalappilly, G.Thibault. (2019). Moving beyond the current limits of data analysis in longevity and healthy lifespan studies. Drug Discovery Today, .
- N. Ho, H. Wu, J. Xu, J.H. Koh, W.S. Yap, W.W.B. Goh, S.C. Chong, S. Taubert, G. Thibault. (2019). ER stress sensor Ire1 deploys a divergent transcriptional program in response to lipid bilayer stress. bioRxiv, 10.1101, 774133.
- Peter Jr. Shyu, Benjamin S.H. Ng, Nurulain Ho, Ruijie Chaw, Seah Yi Ling, Charlie Marvalim, Guillaume Thibault. (2019). Membrane phospholipid alteration causes chronic ER stress through early degradation of homeostatic ER-resident proteins. Scientific Reports, 9, 8637.
- Jhee Hong Koh, Lei Wang, Caroline Beaudoin-Chabot, Guillaume Thibault. (2018). Lipid bilayer stress-activated IRE-1 modulates autophagy during endoplasmic reticulum stress. Journal of Cell Science, 131(22), 1.