Thomas building

Welcome to the Lapointe Lab

Our lab studies one of life’s most fundamental processes: how cells start making proteins. The first step – translation initiation – is tightly regulated to ensure proteins are made in the right quantity at the right time and place. Misregulation of this step is a hallmark of many human diseases, including cancer, neurodegenerative disorders, and inflammatory syndromes. Yet, despite decades of research, we still lack a clear understanding of how translation initiation is carefully controlled.

Featured Publications

eIF1 and eIF5 dynamically control translation start site fidelity Rosslyn Grosely*, Carlos Alvarado*, Ivaylo P. Ivanov, Oliver B. Nicholson, Joseph D. Puglisi, Thomas E. Dever#, and Christopher P. Lapointe#.  2024. bioRxiv preprint 

eIF5B and eIF1A reorient initiator tRNA to allow ribosomal subunit joining. Lapointe CP, Grosely R, Sokabe M, Alvarado C, Wang J, Montabana E, Villa N, Shin B-S, Dever TE, Fraser CS, Fernández IS, and Puglisi JD. 2022. eIF5B and eIF1A. Nature. 607, 185-190.

Dynamic competition between SARS-CoV-2 NSP1 and mRNA on the human ribosome inhibits translation initiation. Lapointe CP, Grosely R, Johnson AG, Wang J, Fernández IS, and Puglisi JD. 2021. Proceedings of the National Academy of Sciences, USA. 118 (6), e2017715118.

Protein-RNA networks revealed through covalent RNA marks. Lapointe CP, Wilinski D, Saunders HAJ, and Wickens M. 2015. Nature Methods. 12, 1163-1170.