The Rho family of GTPases is a subfamily of the Ras superfamily of small (~21 kDa) signaling G proteins. These proteins play a crucial role in regulating various aspects of intracellular actin dynamics, which are essential for cell movement, organelle development, and other cellular functions . The Rho family includes several members, with RhoA, Rac1, and Cdc42 being the most extensively studied .
The identification of the Rho family of GTPases began in the mid-1980s. The first member, RhoA, was isolated in 1985 through a low stringency cDNA screening . Subsequently, Rac1 and Rac2 were identified in 1989, followed by Cdc42 in 1990 . Over the years, additional members were discovered, leading to the identification of 20 mammalian Rho GTPases distributed across eight subfamilies .
Rho GTPases act as molecular switches, cycling between an inactive GDP-bound state and an active GTP-bound state . This switching mechanism allows them to interact with various downstream effectors, thereby regulating multiple cellular processes. The primary functions of Rho GTPases include:
The activity of Rho GTPases is tightly regulated by three classes of proteins:
Human recombinant Rho GTPase 1 is a laboratory-produced version of the naturally occurring protein. It is used extensively in research to study the protein’s structure, function, and role in various cellular processes. Recombinant proteins are produced by inserting the gene encoding the protein into an expression system, such as bacteria or yeast, which then synthesizes the protein in large quantities.
Recombinant Rho GTPase 1 is used in various experimental setups to: