Technology News

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Molecular mechanism that keeps cells in shape identified

Researchers have decoded a molecular mechanism that plays an important role in the development of a cells shape.

London, Dec 4 : Researchers have decoded a molecular mechanism that plays an important role in the development of a cell's shape.

In a human body, cells come in various shapes and sizes. Each cell is shaped in such a way so as to make the best use of it for a specific function. When things go wrong and a cell does not adopt its dedicated shape, its function can be impaired and the cell can cause problems in the body.

The study, conducted by scientists at the European Molecular Biology Laboratory (EMBL) and the Institute for Atomic and Molecular Physics (AMOLF), The Netherlands, elucidated a molecular mechanism that plays a key role in giving a cell its shape.

The study sheds light on the interaction between proteins and the cell's skeleton, that each cell type has its unique shape is due to its cytoskeleton, an internal scaffold built of protein filaments. Especially important are microtubules, dynamic filaments that constantly grow and shrink.

Scientists in the groups of Thomas Surrey and Damian Brunner at EMBL and of Marileen Dogetrom at AMOLF have developed the first method that allows to simultaneously study multiple plus-end tracking molecules, so called +TIPs, in the test tube.

"+TIPs specifically bind to the fast-growing plus end of a microtubule and follow it as it grows. They act as a plus-end label so that other proteins know where to bind to regulate the filament's stability," Nature quoted Surrey, as saying.

"For years it has been impossible to reconstitute this behaviour in a test tube. Our new system now revealed which proteins need to be present for plus-end tracking and what the underlying mechanisms are," he added.

In the study, the researchers applied the new method because of which they succeeded in dissecting a minimal molecular system consisting of three end tracking proteins from yeast cells.

The proteins were labelled with fluorescence to monitor their behaviour with a microscope.

This procedure revealed that one of the proteins has the ability to recognise the specific structure of the growing microtubule tip, binds to it and acts as a loading platform for the other two proteins.

The inherent motor activity of one of the other two proteins, which allows it to walk along microtubules, contributes to the ability of the molecular system to follow growing microtubule ends selectively.

"The great advantage of our new assay is that it can be applied to all kinds of other proteins that interact with microtubules," said Peter Bieling, who carried out the research in Surrey's lab.

"It is a powerful approach that will advance our understanding of the large variety of different microtubule end tracking proteins and can shed light on their mechanics and functions," he added.

The study is published in Nature.

ANI