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.

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Apr 11th, 9:00 AM

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.