作者: Jord C. Stam , John G. Collard
DOI: 10.1007/978-3-642-58591-3_4
关键词: Nuclear transport 、 GTP' 、 Actin cytoskeleton 、 GTPase-activating protein 、 GTPase 、 Guanine nucleotide exchange factor 、 Guanine Nucleotide Dissociation Inhibitors 、 Biology 、 Cell biology 、 Ras superfamily
摘要: Members of the Ras superfamily GTPases play critical roles in regulating a wide range cellular processes, including growth, differentiation, various forms vesicle transport, nuclear transport and actin cytoskeleton regulation (Bourne et al. 1990). These small (about 21 kDa) act as molecular switches that are active when they GTP-bound, inactive GTP is converted to GDP, due their intrinsic GTPase activity (Boguski McCormick 1993). Cycling between conformation influenced by three classes regulatory proteins (Fig. 1). activating (GAPs) stimulate GTPases, thereby accelerating return conformation. Guanine nucleotide exchange factors (GEFs) catalyze release bound GDP which rapidly exchanged GTP, high intracellular ratio free GTP/ vivo. GEFs, also termed guanine dissociation stimulators (GDSs) or (GRFs), induce inhibitors (GDIs) bind stabilize conformation, either GDP-bound-or GTP-bound state In addition, GDIs may extract from membranes, binding GDI carboxyl-terminal isoprene group (Gosser 1997). The localization regulators determine these proteins.