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Conserved nuclear envelope protein uses a shuttle service to travel between job sites
Date:2/10/2014

directly at the Mps3 protein inside living cells and watch for its interactions with Ndc1. To monitor Mps3's interaction with Ndc1, the researchers attached a fluorescent red tag to Ndc1 and a fluorescent green for Mps3. They then focused their microscope on a specific point within a living cell, and watched for green- or red-tagged proteins to enter or leave that space. Their observations would reveal whether Ndc1 and Mps3 were moving independently within the cell, or whether they were physically linked.

"This allowed us to look inside living yeast cells to study the complexes in real time, in the context of the nuclear envelope. We could just sit there and watch, rather than touching or breaking open the cells," Jaspersen says. The imaging not only confirmed the interaction between Mps3 and Ndc1, it allowed the team to track exactly where it occurred.

Although she and her colleagues expected to see Mps3 associate with Ndc1 either at nuclear pore complexes or at the cell's spindle pole bodies, neither turned out to be true. Instead, Mps3 and Ndc1 came together in the nuclear envelope, but away from the two structures the team had set out to study. This led them to speculate that Mps3 might help shuttle Ndc1 to the sites where it is needed, controlling the distribution of nuclear pore complexes and spindle pole bodies. Jaspersen team is now planning further experiments to test how Ndc1 and Mps3 maintain the appropriate balance of these critical structures.


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Contact: Gina Kirchweger
gxk@stowers.org
816-806-1036
Stowers Institute for Medical Research
Source:Eurekalert  

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