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Worm studies shed light on human cancers
Date:4/21/2011

that TFG-1 in the worm controls vesicle formation and secretion out of the ER.

"We found TFG-1 lies at the interface between the ER and the Golgi, in a scaffolding structure called the ER exit site, where it regulates the formation of vesicles carrying their critical cargo," Audhya says.

The research revealed the precise location where TFG-1 does its work and the mechanism by which it spurs unchecked activity.

The scientists demonstrated that human TFG also functions at ER exit sites, which contain a characterized scaffolding protein called Sec16, and likely regulates secretion of multiple cargoes out of cells.

"In the case of one fusion gene, TFG-NTRK-1, the concentrated non-stop activity of NTRK-1 at ER exit sites may cause the first steps that can transform a normal cell into a cancer cell," Audhya says.

The TFG fusions offer a direct target for future "designer" therapies.

"If you identified patients who have fusion genes that express chimeric proteins, you could create a drug that affects only those proteins," he says, adding that TFG fusions leading to chimeric proteins do not exist in healthy people.

Excited about the possibility that their basic science investigations may be applied to several areas of clinical medicine, the researchers have also begun studying TFG as it relates to B-cell development and the secretion of antibodies.


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Contact: Dian Land
dj.land@hosp.wisc.edu
608-261-1034
University of Wisconsin-Madison
Source:Eurekalert

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