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
Department
Chemistry
Location
Henry Hall Atrium 2
Start Date
11-4-2012 9:00 AM
Keywords
Physical Science
Abstract
Diaphanous-related formins are a conserved family of proteins that affect many cellular processes by regulating cytoskeletal dynamics. Formins nucleate actin filaments by recruiting actin monomers as the filament elongates. Since the formins influence so many cellular processes, it is vital that they are tightly regulated. The regulation of one specific mammalian formin, mDia2, occurs by intramolecular interactions. Autoinhibitory binding to prevent actin polymerization occurs between the diaphanous inhibitory domain (DID) at the N-terminus and the diaphanous auto regulatory domain (DAD) at the C-terminus. It is understood that formins are activated by a Rho GTPase, but this binding may not fully activate the protein. Previously, we showed that p21 activated kinase (PAK1) phosphorylates mDia2 and potentially regulates formins. We have performed isothermal titration calorimetry and actin polymerization assays to characterize the mechanism for phosphorylation of mDia2 with PAK1.
Probing the Role of Phosphorylation in the Mechanism of Formin mDia2
Henry Hall Atrium 2
Diaphanous-related formins are a conserved family of proteins that affect many cellular processes by regulating cytoskeletal dynamics. Formins nucleate actin filaments by recruiting actin monomers as the filament elongates. Since the formins influence so many cellular processes, it is vital that they are tightly regulated. The regulation of one specific mammalian formin, mDia2, occurs by intramolecular interactions. Autoinhibitory binding to prevent actin polymerization occurs between the diaphanous inhibitory domain (DID) at the N-terminus and the diaphanous auto regulatory domain (DAD) at the C-terminus. It is understood that formins are activated by a Rho GTPase, but this binding may not fully activate the protein. Previously, we showed that p21 activated kinase (PAK1) phosphorylates mDia2 and potentially regulates formins. We have performed isothermal titration calorimetry and actin polymerization assays to characterize the mechanism for phosphorylation of mDia2 with PAK1.