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.
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.