IRIC - Institute for Research in Immunology and Cancer

Published on March 5, 2024

Cell division, a process required for the survival of all species, enables the genetic material of a mother cell to be separated and shared between its two daughter cells. As many aspects of cell division remain poorly understood, the team led by Jean-Claude Labbé, Director of the Cell Division and Differentiation Research Unit, focused on one of its final stages, cytokinesis. The team identified a new protein, OSGN-1, as being required for the correct completion of cell division. The study, published in the journal PNAS, was led by research associate Eugénie Goupil and doctoral student Léa Lacroix.

A required oxygenase activity

Through experiments with the nematode C. elegans, the team identified a new protein required for cell division: the enzyme OSGN-1, which potentially possesses the ability to add an oxygen atom to other proteins (oxygenase activity). The enzymatic activity of OSGN-1 was shown to be required to maintain cell organization during division. In the absence of OSGN-1, cells fail to divide and end up with twice their genetic material. This polyploidy can lead to cell instability and dysfunction.

A protein present in human cells

The team found that a protein with the same activity as OSGN-1 was present in human cells: the OSGIN1 protein. This suggests a conserved activity throughout the evolution of animal species.

The identification and characterization of OSGN-1 in C. elegans and OSGIN1 in humans reveals a novel activity required and conserved to ensure the completion of cell division. Since cells that possess a double amount of genetic material are more likely to acquire tumoral properties, OSGN-1/OSGIN1 could be involved in the development of certain forms of cancer.

Cited study

Goupil, E., Lacroix, L., Brière, J., Guga, S., Saba-El-Leil, M.K., Meloche, S., and Labbé, J.-C. (2024). OSGN-1 is a conserved flavin-containing monooxygenase required to maintain intercellular bridge stability in late cytokinesis. Proc. Natl. Sci. USA. 121 (11) e2308570121