LRI scientists identify new cytokinesis regulatory mechanism
 Scientists in the London Research Institute's Protein Phosphorylation group, led by Peter J Parker, have identified a new regulatory mechanism that controls exit from cytokinesis.
Cytokinesis, where a cell divides into two daughter cells, is an exquisitely regulated process that has evolved to ensure a high degree of fidelity. The current understanding of the internal cellular 'checks', that are applied to ensure each step in this complex biological process is completed in an orderly fashion, has largely focussed on the copying of the genetic material and the associated increase in size of the mother cell as it approaches the point of division. However there are many critical steps in this division cycle, not least of which is the final step of separation, which yields the two daughter cells.
This sophisticated final step, irreversibly separates the two daughter cells removing any opportunity to redistribute (incorrectly apportioned) cellular contents. Errors in this final step can lead to aberrant genetic content in daughter cells - a feature that can be a prelude to cancer.
The group's discovery of this new regulatory mechanism has been published in the Nature Cell Biology *. The paper describes a hitherto unidentified regulator that exerts its action to control this final step in the process of division - when this regulator is dysfunctional the mother cell frequently fails to divide causing an accumulation of cells with double the normal genetic content. Such (polyploid) cells, if they survive, can lead to cancer.
Image caption: A specific cellular signal (in red), that we show is critical for cell separation, is only turned on in cells undergoing division.
* Saurin AT, Durgan J, Cameron AJ, Faisal A, Marber MS, Parker PJ. The regulated assembly of a PKCε complex controls the completion of cytokinesis. Nature Cell Biology 2008; doi:10.1038/ncb1749 (Epub ahead of print).
Abstract in PubMed | Advance publication in Nature Cell Biology
For more information on Peter J Parker and the Protein Phosphorylation group, see Peter Parker's research profile.
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