Scientists at The Scripps Research Institute have solved the structure of Piezo1, a protein that helps convert physical stimuli into chemical signals. The work was published yesterday in Nature

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Piezos are ion channels that let ions through a pore in response to mechanical stimuli such as touch. In this new study, researchers use cryo-electron microscopy to examine the structure of Piezo1 and how the parts came together. They found that Piezo1 is made up of three curved "blades" circling a central pore and believe these blades move in response to a mechanical force. A beam-like structure serves as the backbone for each blade. An "anchor domain" surrounds the pore where the blades meet the middle.

"It is a beautiful structure," says Ardem Patapoutian, Ph.D. "The features identified in this study give us tantalizing clues on how this ion channel would sense and respond to membrane tension."

Andrew Ward, Ph.D. says the structure of Piezo1 is unique because it appears to be an "all-in-one" protein, meaning it does not need to connect with other proteins or cell structures to do its job transmitting a signal.

The team's next step is to examine the overall architecture of Piezo1 and determine how each piece works. 

Image: Structure of Piezo1, showing two of the three blades that surround the central pore. Image courtesy of the Ward Lab.