PP1 Inhibitor 2 in Zebrafish
Poster Number
51
Format
Poster Presentation
Faculty Mentor Name
Doug Weiser
Faculty Mentor Department
Biological Sciences
Abstract/Artist Statement
Protein phosphatase 1 (PP1) is essential regulator of the control of glycogen metabolism, muscle contraction, cell division and regulation of membrane receptors and channels. Regulation of these processes is through PP1 holoenzymes that facilitates the PP1 catalytic subunit. These holoenzymes consists, of different regulatory and inhibitory subunits along with the catalytic subunit. Protein phosphatase inhibitor-2 (I-2) is one of the earliest discovered inhibitors, but still much is not known about it and it’s role in vivo. The main topic of research is how it binds to certain PP1 subunits and not others. A goal of our project is to examine and potentially develop zebrafish I-2 as a genetic model system. Inhibition by I-2 is used to distinguish PP1 activity from other phosphatases. Due to lack of research on this inhibitor we are running controls in order to purify the protein and then run experiments on the same inhibitor in zebrafish. We are currently trying to see the differential interactions of I-2 with various PP1 holoenzymes. Recombinant human I-2 was purified from E. Coli. A pull down with GST I-2 and GST was done against a series of PP1 regulatory subunits: Gadd34, GaddRVXF (non PP1 binding mutant), Flag-Neurabin, Flag-Crep and MYPT1. This GST-pull down will be able to distinguish with ones bind and which do not, which will allow us to examine the evolutionary conservation of I-2 function.
Location
DeRosa University Center, Ballroom
Start Date
20-4-2013 1:00 PM
End Date
20-4-2013 3:00 PM
PP1 Inhibitor 2 in Zebrafish
DeRosa University Center, Ballroom
Protein phosphatase 1 (PP1) is essential regulator of the control of glycogen metabolism, muscle contraction, cell division and regulation of membrane receptors and channels. Regulation of these processes is through PP1 holoenzymes that facilitates the PP1 catalytic subunit. These holoenzymes consists, of different regulatory and inhibitory subunits along with the catalytic subunit. Protein phosphatase inhibitor-2 (I-2) is one of the earliest discovered inhibitors, but still much is not known about it and it’s role in vivo. The main topic of research is how it binds to certain PP1 subunits and not others. A goal of our project is to examine and potentially develop zebrafish I-2 as a genetic model system. Inhibition by I-2 is used to distinguish PP1 activity from other phosphatases. Due to lack of research on this inhibitor we are running controls in order to purify the protein and then run experiments on the same inhibitor in zebrafish. We are currently trying to see the differential interactions of I-2 with various PP1 holoenzymes. Recombinant human I-2 was purified from E. Coli. A pull down with GST I-2 and GST was done against a series of PP1 regulatory subunits: Gadd34, GaddRVXF (non PP1 binding mutant), Flag-Neurabin, Flag-Crep and MYPT1. This GST-pull down will be able to distinguish with ones bind and which do not, which will allow us to examine the evolutionary conservation of I-2 function.