Transport of vesicles within the cell, and vesicle-mediated secretion and uptake, through GTPase control of vesicle coat assembly. GTPases are active when bound to GTP and inactive when bound to GDP.

GAPs (GTPase activating proteins) catalyse the return to the inactive GDP-state, by stimulating an otherwise low intrinsic GTPase activity. (B) Ras activation at the leading edge of chemotaxing cells.

Keywords: Translation, Ribosome, GTPase, Rbg1, Rbg2, Tma46, Gir2. Introduction. The developmentally regulated GTP-binding (DRG) proteins are a family of highly conserved GTPases that consists of two closely related paralogs: DRG1 and DRG2 (Fig. 1) .

Jan 1, 2019 · Small GTPase is a kind of GTP-binding protein commonly found in eukaryotic cells. It plays an important role in cytoskeletal reorganization, cell polarity, cell cycle progression, gene expression and many other significant events in cells, such as …

The GTPase reaction is of great medical significance, since any disruption of this reaction such as that caused by inhibitory mutations in genes encoding GAP proteins results in persistent downstream signaling.

Nov 9, 2018 · These ubiquitous enzymes operate by hydrolyzing GTP to GDP with associated conformational changes that modulate affinity for family-specific binding partners. There are three major GTPase superfamilies: Ras-like GTPases, heterotrimeric G proteins and protein-synthesizing GTPases.

At least two alternative mechanisms for activation of the oncogenic potential of GTPases have been found. Point mutations that reduce their GAP-stimulated GTPase activity would render proteins with a much lower efficiency to catalyse GTP hydrolysis.

A GTPase is an enzyme that facilitates the conversion of guanosine triphosphate (GTP) to guanosine diphosphate (GDP). It plays a crucial role in regulating various cellular processes such as cell growth, differentiation, migration, and vesicle trafficking.

The members of the Rho GTPase family have been shown to regulate many aspects of intracellular actin dynamics, and are found in all eukaryotic kingdoms, including yeasts and some plants. Three members of the family have been studied in detail: Cdc42, Rac1, and RhoA.

The rate of GTP hydrolysis for small GTPases is generally too slow to create physiologically relevant transient signals, and thus requires another class of regulatory proteins to accelerate this activity, the GTPase activating proteins (GAPs).