
This image shows the domain structure of p27, an intrinsically disordered protein.
Like a baseball player itching to steal second base, cell division advances in part thanks to the fluctuations of a key regulatory protein. Researchers in Memphis and Europe used the latest technologies to capture the critical motions. The results provide clues about how proteins do their jobs. The findings also offer insight into uncontrolled cell division, which is a hallmark of cancer.
Researchers focused on the protein p27. Most proteins fold into a set shape, but p27 does not. The protein remains flexible and disordered. That lets p27 rapidly change its shape and function as the cells’ needs change.
In one shape, p27 prevents cell division. When cells need to divide, p27 must change again. Researchers showed that the flexibility and fluctuations of key segments of p27 make that change possible.
“The key insight in this study is that even though p27 appeared to be locked into a rigid shape that prevents cell division, there are regions of the protein that fluctuate enough to get the process started,” said Richard Kriwacki, PhD, of the St. Jude Department of Structural Biology.
Nature Communications published a report on this work.
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