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At busy intersections, traffic signals usually help the road to maintain its maximum volume to keep traffic flowing.
, cell division in the body is regulated by proteins that control how cells divide, move, and protect themselves from stress.
recently, Rohit V. Pappu, a professor of engineering at the University of Washington's School of Engineering and Applied Sciences, and his former postdoctoral researcher, Rahul Das, worked with Richard Kriwacki of St. Jude Children's Research Hospital and his team to reveal the molecular logic of how quickly cancer cells can be prevented from splitting.
related findings published in the recent pNAS journal.
the team studied the p27 protein, which is tasked with preventing cell division or slowing its division.
Pappu says this is an important job because genetic mutations in p27 and other similar proteins are a major culprit in cancer. "Understanding how p27 inhibitors act as 'cell cycle inhibitors' is key to understanding how p27 simulates compounds that prevent cell proliferation and growth, a key feature of human cancer,"
Pappu said.
" In early work, Kriwacki's team showed that the presence of p27 could be a stop sign of cell division.
by adding a phosphate base to modify a key amino acid, the degradation of p27 can be initiated, which allows p27 to enter the cell's trash can, removing the stop sign and allowing the cell to continue to divide.
collaboration between Pappu and Kriwacki Labs, began to revolve around a common interest, the so-called inner disordered protein.
different from traditional proteins, p27 and other inherently disordered proteins do so without having to fold into well-defined three-dimensional structures.
2013, Pappu and Das, now a bioinformatics scientist at the Rothberg Institute for Childhood Illness and a visiting scholar at the Yale Cancer Center, found that the shape and size of the inherent disordered proteins were regulated by the pattern of positive and negative chargeaminos in a linear sequence.
discovery opens up a design strategy in which researchers studied the effects of changes in the residual pattern of reverse charge on the efficiency of phosphorylation in a specific amino acid that controls the degradation of p27 and stops cell division. "All variants of the design improve the phosphorylation efficiency of p27, which means that the naturally occurring sequence pattern has evolved to ensure a more durable stop signal marker," said
Pappu.
" Pappu said the results could help his team and other scientists discover the molecular logic of cell cycles and other cellular processes controlled by internal disordered proteins. "We've designed a strategy that can be applied to a variety of systems to understand the molecular logic of how these disordered proteins function," says
Pappu.
this will allow us to understand the regulatory mechanisms of the molecular switches that affect cell division, cell movement, and programmed cell death.
" Source: Decoding Medicine.