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A cascade involving p85, Cdc42 and septin 2 regulates cytokinesis.

Mitosis, the final phase of cell division, includes the processes of nuclear division and cytosolic division (cytokinesis). Cytokinesis occurs when DNA separation terminates, and involves a number of proteins that induce furrowing at the region of cell separation, formation of new membrane, and abscission. This process is remarkably complex, and the list of proteins that regulate it is long. Our understanding is limited as to how these players are organized in space and time to ensure that the cytosol divides equally, and only after nuclear division. Class I(A) PI3K (phosphoinositide 3-kinase) is an enzyme activated by growth factor receptor stimulation, but it is re-activated in early mitosis and regulates mitosis entry. By the end of mitosis, PI3K activity is low; at this point, the class I(A) PI3K regulatory subunit p85 contributes to co-ordination of the cytoskeletal changes required for cytokinesis. The impact of these observations on current models of cytokinesis execution is discussed here.[1]

References

  1. A cascade involving p85, Cdc42 and septin 2 regulates cytokinesis. Silió, V., Marqués, M., Cortés, I., Zuluaga, S., Carrera, A.C. Biochem. Soc. Trans. (2007) [Pubmed]
 
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