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Nanoresearchers challenge dogma in protein transportation in cells
Date:9/21/2009

- We now begin to understand how signalling proteins recognize and transport to certain areas of the cell and get a more clear insight on the mechanism of major cellular processes such as cell signalling and growth. This valuable knowledge could be used in the future to understand and cure disease such as depression and Alzheimer's explains Associate Professor Dimitrios Stamou, Nano-Science Center and Department of Neuroscience and Pharmacology, who led the work.

Cells depend critically on their ability to selectively, transport and isolate proteins in specific areas. Earlier ideas that proposed proteins to move around in the cell by recognizing nanoscale patches in their surrounding membrane, also called lipid rafts, are currently under intense debate. However researchers from Nano-Science Center found a new unsuspected mechanism based on the shape of the membrane and just had their results published in the prominent scientific journal Nature Chemical Biology.

Attractive curves on the nanoscale

Like all other materials, cell membranes will crack when bend. Membranes however show a unique property: bending them more and more does not create bigger cracks but simply many more cracks of the same size. It turns out certain important proteins "like" to bind in these cracks therefore the curved parts of a membrane become a good place for them to "meet" each other and thus perform the complicated tasks that need many different proteins working side by side.

- We were very surprised that it is the number of cracks in the membrane that determines how many proteins are bound. Up until now researchers in the field thought that the crucial element was the proteins ability and "desire" to bind to the membrane, also called the affinity. Our data speaks against that, explains Nikos Hatzakis, Nano-Science Center and Department of Chemistry.

The model is general

In cells proteins are travelling around i
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Contact: Dimitrios Stamou
stamou@nano.ku.dk
454-116-0468
University of Copenhagen
Source:Eurekalert

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