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'Shuttling' protein possibly key to resilience of cancer cells

un protein to be produced, attracting more ATF2 and reinforcing the localization of ATF2 in the nucleus.

Because it has been reported that ATF2 overexpression causes the resistance of cancer cells to chemotherapy and radiation, the ATF2 shuttling might play a key role in the ability of cancer cells to resist cancer treatments, and preventing the ATF2 from moving into the cytoplasm might improve the effectiveness of anticancer treatments.

"Ultimately, we are trying to figure out how to make the cancer cells more sensitive to chemotherapy and radiation treatment by keeping the ATF2 in the nucleus," Hu said.

The Purdue researchers tracked ATF2 and other proteins using a fluorescent imaging technique developed by Hu called bimolecular fluorescence complementation. The procedure involves breaking a fluorescent protein into two fragments and then fusing each fragment to different AP-1 proteins, including c-Jun and ATF2. When the proteins later bind to form a heterodimer, the fluorescent-protein fragments are reunited, causing them to glow green when illuminated with a light source. The fluorescence enabled the researchers to pinpoint the location of c-Jun-ATF2 heterodimers and discover the shuttling movements of ATF2. The ATF2 protein also has been found in the cytoplasm of diseased brain cells in Alzheimer's disease and muscle cells in the heart, suggesting the same shuttling mechanism might be involved in those conditions.

"These findings suggest a new avenue to study how ATF2 is implicated in the pathogenesis of these diseases," Hu said.


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Source:Purdue University


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