Cellular Regulation of the Formin Protein, DAAM1

Presentation Type

Poster/Portfolio

Presenter Major(s)

Cell and Molecular Biology

Mentor Information

Brad Wallar

Department

Chemistry

Location

Kirkhof Center KC2

Start Date

11-4-2012 9:00 AM

Keywords

Life Science

Abstract

Formins are a family of proteins responsible for cytoskeletal organization by playing an integral role in actin nucleation and polymerization. Dishevelled-Associated Activator Morphogenesis 1 (DAAM1) is a formin found in all mammalian organisms and consists of several domains. Two of these domains, the Diaphanous Autoregulatory Domain (DAD) and the Diaphanous Inhibitory Domain (DID) bind to each other to inactivate the protein. Activation occurs when DID-DAD interactions are disrupted by the binding of active Rho GTPase to the N-terminus of DAAM1. Once activated, DAAM1 is believed to act as a guanine nucleotide exchange factor (GEF) for the Rho GTPase. However, a new possible component of this pathway, a known Rho GEF, NET1, could be activating Rho instead of DAAM1. An alternative binding relationship was discovered between DAAM1, Dvl, and NET1. Being a known Rho GEF makes NET1 a strong candidate in Rho activation, leading to a new role in cytoskeletal regulation.

This document is currently not available here.

Share

COinS
 
Apr 11th, 9:00 AM

Cellular Regulation of the Formin Protein, DAAM1

Kirkhof Center KC2

Formins are a family of proteins responsible for cytoskeletal organization by playing an integral role in actin nucleation and polymerization. Dishevelled-Associated Activator Morphogenesis 1 (DAAM1) is a formin found in all mammalian organisms and consists of several domains. Two of these domains, the Diaphanous Autoregulatory Domain (DAD) and the Diaphanous Inhibitory Domain (DID) bind to each other to inactivate the protein. Activation occurs when DID-DAD interactions are disrupted by the binding of active Rho GTPase to the N-terminus of DAAM1. Once activated, DAAM1 is believed to act as a guanine nucleotide exchange factor (GEF) for the Rho GTPase. However, a new possible component of this pathway, a known Rho GEF, NET1, could be activating Rho instead of DAAM1. An alternative binding relationship was discovered between DAAM1, Dvl, and NET1. Being a known Rho GEF makes NET1 a strong candidate in Rho activation, leading to a new role in cytoskeletal regulation.