Study unveils the intricate way two proteins interact to promote cell movement, metastasis | 10/3/2019 | Staff
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The cryo-EM 3D reconstruction (left) of the protein P-Rex1 bound to Gβγ and the proteinmodel (right) showing that Gβγ (top; blue and green) binds to a compact, multi-domain surfaceon P-Rex1 (bottom; yellow, magenta, teal and gold). Credit: Jennifer Cash, U-M LifeSciences Institute.

When cells in our bodies need to move—to attack an infection or heal a wound, for example—cellular proteins send and receive a cascade of signals that directs the cells to the right place at the right time. It's a process cancer cells can hijack to spread to new tissues and organs.

Team - Researchers - University - Michigan - Life

Now, a team of researchers led by the University of Michigan Life Sciences Institute has shed light on a key driver of this process. The findings, scheduled to publish Oct. 16 in Science Advances, offer important insights into cell migration not only under normal health conditions, but also in breast, prostate and other types of cancers.

The researchers specifically probed a protein called P-Rex1 (phosphatidylinositol 3,4,5-triphosphate-dependent Rac exchanger 1), which is activated when it binds another protein, Gbg. Despite the discovery of P-Rex1 more than 15 years ago, precisely how the two proteins interact and how this interaction leads to cell movement has remained poorly understood.

Combination - Biology - Biochemistry - Techniques - Researchers

Using a combination of structural biology and biochemistry techniques, the researchers have revealed the structure of P-Rex1 bound to Gbg, providing a snapshot of how this intricate activation process unfolds.

"Knowing the structure of this protein complex provides mechanistic details that allow us to understand how it is regulated," said Jennifer Cash, LSI researcher and lead author of the study. "And when we understand how it's regulated, we can start to think about how to modify that regulation and inhibit P-Rex1 signaling in cancers."

Team - Gbg - Surface

The team found that Gbg binds to an extensive surface on...
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