title: New insight into the molecular switch mechanism of human Rho family proteins: shifting a paradigm.
abstract: Major advances have been made in understanding the structure, function and regulation of the small GTP-binding proteins of the Rho family and their involvement in multiple cellular process and disorders. However, intrinsic nucleotide exchange and hydrolysis reactions, which are known to be fundamental to Rho family proteins, have been partially investigated in the case of RhoA, Rac1 and Cdc42, but for others not at all. Here we present a comprehensive and quantitative analysis of the molecular switch functions of 15 members of the Rho family that enabled us to propose an active GTP-bound state for the rather uncharacterized isoforms RhoD and Rif under equilibrium and quiescent conditions.
authors.affiliation: Institut für Biochemie und Molekularbiologie II, Medizinische Fakultät der Heinrich-Heine-Universität, D-40225 Düsseldorf, Deutschland.
authors.forename: Mamta
authors.initials: M
authors.lastname: Jaiswal
authors.forename: Eyad Kalawy
authors.initials: EK
authors.lastname: Fansa
authors.forename: Radovan
authors.initials: R
authors.lastname: Dvorsky
authors.forename: Mohammad Reza
authors.initials: MR
authors.lastname: Ahmadian
mesh_terms: D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D020741:rho GTP-Binding Proteins / Q000737:chemistry / Q000145:classification / Q000378:metabolism*
chemical_list: D006160:Guanosine Triphosphate; D020741:rho GTP-Binding Proteins