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UVa researchers describe method of protecting chromosomes during cell division

totic centromere-associated kinesin) onto the chromosome in an inactive state. When a microtubule from the wrong side of the cell binds a chromatid, MCAK is activated and removes the improperly attached microtubule.

"Aurora B is a regulatory protein that has been previously implicated in this process," Stukenberg said. "It is very satisfying to find that a protein which it is regulating has the enzymatic activity required to remove improperly-attached microtubules. Many questions remain, however, and we at U.Va. are focusing on how MCAK is activated by improper attachments."

Aurora B is a kinase that regulates proteins by modifying amino acids. The researchers identified the specific amino acid on MCAK that was modified by Aurora B, and showed that the modification regulates MCAK activity. Cell injection studies showed the sites where this modification happens, which is crucial for the correct attachment of chromatids and microtubules during mitosis. The researchers also stained cells by immunofluorescence with antibodies to MCAK, phosphorylated MCAK and Aurora B, suggesting that Aurora B regulates MCAK to destroy incorrectly attached microtubules.

Early in the 20th century, some scientists proposed that aneuploidy may be one cause of cancer, Stukenberg said, but that theory was largely ignored for many years.

Now, recent research has "reinvigorated the theory," he said. "So it is important to study whether mutations in Aurora, MCAK or the inability to resolve improper microtubule attachments, is involved in tumor genesis. It is already clearly established that the Aurora family of kinases is overexpressed in many cancerous solid tumors."


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Contact: Bob Beard
reb8e@virginia.edu
434-982-4490
University of Virginia Health System
4-Mar-2004


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