At the Institut Curie, two CNRS teams have just reported crucial information on the orientation of cells as they divide. The cell division axis determines not only the position of the daughter cells but also their contents and hence their fate. The researchers have shown that the orientation of division depends on focal adhesions of the cell with its surroundings. They have also identified a new molecule that controls the localization of cellular determinants of so-called asymmetric cell division, thus giving rise to two different cells.
These two studies published in the October and November 2005 issues of Nature Cell Biology shed new light on one of the essential mechanisms in the life of a cell whose deregulation may give rise to cancer.
Division is an essential stage in the life of all cells: it participates in the body’s growth, wound repair, combating infection and in cell turnover. Within our bodies at any given moment some 250,000 million cells are dividing, that is 250,000 million mother cells are in the process of forming 500 000 million daughter cells. As individuals, however, we observe no change. This is because each newly formed cell has a well determined location. The mother cell has a given place among other cells in a tissue and, to avoid perturbing this organization, the daughter cells it produces are also appropriately placed. This very precise positioning is indispensable in maintaining the shape of our tissues and organs. The constraints imposed by the environment influence the division and position of the daughter cells.
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
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