Optimized by nature over 100 million years of evolution, a smart liquid provides a crucial coupling that ensures cell division correctly proceeds. Scientists from Paul Scherrer Institute and ETH Zurich have uncovered the mechanism by which proteins form small liquid droplets that act as a smart adh
have uncovered the mechanism by which proteins form small liquid droplets that act as a smart adhesive in cells. These droplets attach to the ends of microtubules, which helps position the cell’s nucleus correctly during division. The research, published in, explain the long-standing mystery of how moving protein structures in cells are joined together.
By forming a liquid droplet, the proteins achieve the perfect material properties to ensure biological function. This discovery is just the beginning of a new understanding of the role smart liquids play in the cell, believes Barral, whose research group is investigating the process of cell division in yeast.
One question that had long intrigued scientists was how the three core Kar9 network proteins stay attached to the microtubule tip even when tubulin subunits are added or removed: equivalent to the hook at the end of a towrope remaining in place whilst adjacent sections of rope are inserted or snipped off.
In solution, the three proteins came together to form distinct droplets, like oil in water. To prove that this was occurring in yeast cells, the researchers investigated the effect of mutations on cell division and the ability of the proteins to track the end of a shrinking microtubule.
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