When cells in a human body need to move—to attack infection or heal a wound, for instance—cellular proteins send and receive rapids of signals that direct the cells to the right place at the right time. It is a process cancer cells can follow to spread to new tissues and organs.
Now, a group of research professors led by the University of Michigan Life Sciences Institute has shed light on a critical driver of this process. The conclusions, scheduled to publish Oct. 16 in Science Advances, offer necessary insights into cell movement not only under normal health conditions but also in the breast, prostate, and other kinds of cancers.
The researchers specifically examined a protein known as P-Rex 1, which is activated when it binds another protein, Gbg. Despite the invention of P-Rex1 over 15 years ago, precisely how the two proteins work together and how this interaction leads to cell movement has remained poorly known.
Utilizing a combination of structural biology and biochemistry techniques, the researchers have revealed the structure of P-Rex1 bound to Gbg, offering a snap of how this intricate activation process unfolds.
The group found that Gbg binds to an extensive surface on P-Rex1 comprised of a number of different protein domains. Earlier studies offered conflicting arguments about which domain bound Gbg. However, this newest study was capable of resolving the dispute by taking a bigger-image of the protein, using newer technologies.