Event Title
Probing the Role of Phosphorylation in the Mechanism of Formin mDia2
Presentation Type
Poster/Portfolio
Presenter Major(s)
Chemistry
Mentor Information
Brad Wallar, wallarb@gvsu.edu
Department
Chemistry
Location
Henry Hall Atrium 53
Start Date
13-4-2011 10:00 AM
End Date
13-4-2011 11:00 AM
Abstract
Diaphanous-related formins are a highly conserved family of proteins that influence numerous cellular processes by regulating the cytoskeleton. However, since the formins are an important focal point which affect so many cellular processes, it is vital that they are tightly regulated and only activated in response to cellular signals, as uncontrolled formins can result in dire consequences for a cell. The regulation of one specific mammalian formin, mDia2, involves the two ends of the protein binding to each other to keep it in an inactive complex. We have identified a specific cellular protein (PAK1) that phosphorylates mDia2 and potentially serves to activate the formin in cells. We have also identified the specific amino acid sites on mDia2 that are modified by PAK1. Using a combined approach of site-directed mutagenesis, protein biochemistry, isothermal titration calorimetry, and fluorescence anisotropy, we have discovered a novel mechanism of formin protein regulation in cells.
Probing the Role of Phosphorylation in the Mechanism of Formin mDia2
Henry Hall Atrium 53
Diaphanous-related formins are a highly conserved family of proteins that influence numerous cellular processes by regulating the cytoskeleton. However, since the formins are an important focal point which affect so many cellular processes, it is vital that they are tightly regulated and only activated in response to cellular signals, as uncontrolled formins can result in dire consequences for a cell. The regulation of one specific mammalian formin, mDia2, involves the two ends of the protein binding to each other to keep it in an inactive complex. We have identified a specific cellular protein (PAK1) that phosphorylates mDia2 and potentially serves to activate the formin in cells. We have also identified the specific amino acid sites on mDia2 that are modified by PAK1. Using a combined approach of site-directed mutagenesis, protein biochemistry, isothermal titration calorimetry, and fluorescence anisotropy, we have discovered a novel mechanism of formin protein regulation in cells.