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Mitosis mystery solved as role of key protein is confirmed

Mitosis mystery solved as role of key protein is confirmed - 19 February 2014. iStock
News from: The University of Warwick

Researchers from Warwick Medical School have discovered the key role of a protein during cell duplication, answering a question that has evaded scientists for half a century.

Restarted endocytosis in a mitotic cell. Image: Royle/University of Warwick
Restarted endocytosis in a mitotic cell.
Image: Royle/University of Warwick

The BBSRC-funded study, published in the journal eLife, is the first to outline the role of a protein called actin in shutting down clathrin-dependent endocytosis during mitosis, as a cell divides into two identical copies.

Endocytosis is the process by which cells absorb molecules that are too large to pass through the plasma membrane, such as proteins. Clathrin-dependent endocytosis is the most common route for this. Clathrin, a protein, forms a pit on the inner surface of the membrane which allows the cell to engulf and bring in a small volume of fluid from outside the cell.

Endocytosis shuts down during mitosis, but the understanding of why it happens has eluded researchers until now.

The Warwick team found that during mitosis, actin is used to help form a stiff cortex in the cells and cannot be recruited for endocytosis. In other words, actin is needed, but is unavailable for use.

By tricking the cell into making actin available during mitosis, the researchers were able to restart endocytosis in mitotic cells.

The discovery opens the door for further developments, both for researchers and for possible clinical applications.

Dr Steve Royle, who led the research team, said: "The implications for human health are truly fascinating; by knowing the role played by actin we can look to use it to restart endocytosis during cell division. That could mean that we're able to make dividing cells receptive to pharmaceuticals or other medical treatments in a way that we haven't before."

ENDS

Notes to editors

For further information, a copy of the full paper, or to arrange interviews with Dr Royle please see external contact below.

From 18 February 2014, the paper is available at: elife.elifesciences.org/content/3/e00829.