Asst. Prof. Suzuki, Sho
Nanyang Assistant Professor
Phone: (65) 6316 2809
Email: [email protected]
Personal Lab Webpage: https://sites.google.com/view/shosuzuki
Eukaryotic cells compartmentalize biochemical processes within membrane-bound organelles, yet these organelles communicate through membrane contact sites (MCSs)—specialized regions critical for signaling and lipid exchange. The Suzuki Lab studies how MCSs contribute to membrane remodeling events such as fusion, fission, tubulation, and vesicle formation, which remain poorly understood. Recent work uncovered a novel pathway linking ER–endosome contacts to multivesicular body (MVB) biogenesis via the ESCRT complex (Suzuki et al., J. Cell Biol. 2024). The lipid transport protein VPS13 bridges the ER and endosomes, supplying lipids required for intralumenal vesicle formation. These findings offer new insight into lipid dynamics at MCSs. Using cell biology, biochemistry, advanced imaging, and genetics, the lab investigates the molecular principles of organelle interaction and remodeling. It also explores how mutations in MCS-resident proteins like VPS13 underlie diseases such as Parkinson’s, aiming to inform therapeutic strategies.
Research Areas
cell biology, organelle contact sites, membrane dynamics, super-resolution, in vitro reconstitution
PhD Student
PhD Student
PhD Student
Research Engineer
- Qi, Y., and Suzuki, S.W. "TEX264-mediated selective autophagy directs DNA damage repair." Trends in Biochemical Sciences 50, no. 3 (2025): 190–202. https://doi.org/10.1016/j.tibs.2024.10.012
- Suzuki, S.W., West, M., Zang, Y., Fan, J.S., Roberts, R.T., Odorizzi, G., and Emr, S.D. "A role for Vps13-mediated lipid transfer at the ER-endosome contact site in ESCRT-mediated sorting." Journal of Cell Biology 223, no. 1 (2024): e202307094. https://doi.org/10.1083/jcb.202307094
- Suzuki, S.W., Oishi, A., Nikulin, N., Jorgensen, J.R., Baile, M.G., and Emr, S.D. "A PX-BAR protein Mvp1/SNX8 and a dynamin-like GTPase Vps1 drive endosomal recycling." eLife 10 (2021): e69883. https://doi.org/10.7554/eLife.69883
- Suzuki, S.W., Yamamoto, H., Oikawa, Y., Kondo-Kakuta, C., Kimura, Y., Hirano, H., and Ohsumi, Y. "Atg13 HORMA domain recruits Atg9 vesicles during autophagosome formation." Proceedings of the National Academy of Sciences USA 112, no. 7 (2015): 3350–3355. https://doi.org/10.1073/pnas.1421092112
- Fujioka, Y., Suzuki, S.W., Yamamoto, Y., Kondo-Kakuta, C., Kimura, Y., Hirano, Y., Akada, R., Inagaki, F., Ohsumi, Y., and Noda, N.N. "Structural basis of starvation-induced assembly of the autophagy initiation complex." Nature Structural & Molecular Biology 21, no. 9 (2014): 513–521. https://doi.org/10.1038/nsmb.2822