Words similar to gtp-bound
Example sentences for: gtp-bound
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Rab proteins comprise a large family of Ras-related GTPases that function in the anterograde and retrograde trafficking of proteins in mammalian cells [ 1 2 3 ] . Different Rab proteins reside in specific subcellular membranes or organelles, where they mediate vesicular transport between discrete donor and acceptor compartments in the endocytic or exocytic pathways [ 4 5 ] . Detailed studies of a few Rab proteins ( e.g .; Rab1, Rab5 and Rab9) have led to a general model wherein Rab proteins are presumed to cycle on and off donor and acceptor membranes in connection with changes in their guanine nucleotide state [ 6 7 8 ] . In the active GTP-bound state, Rab proteins associate with budding transport vesicles [ 9 10 11 ] and appear to participate in the assembly of membrane docking complexes [ 12 13 14 ] . Following vesicle fusion with the acceptor compartment and GTP hydrolysis, the inactive GDP-bound Rab is extracted from the membrane by a carrier protein termed guanine nucleotide dissociation inhibitor (GDI) [ 15 16 17 ] . The GTPase can then re-enter the transport cycle through nucleotide exchange promoted by a specific exchange factor at the donor vesicle membrane [ 18 19 20 ] . In addition to changes in guanine nucleotide state, the posttranslational prenylation of Rab proteins plays an important role in the cycling mechanism.
2C), we were surprised to find that the S22N mutant was predominantly in the GTP-bound state.
The functions of Boi1/Boi2 appear to be linked to those of Cdc42 and Rho3, which are Rho-type GTPases that are important for polarized cell growth [ 4 5 6 7 8 9 ] . Boi1 and Boi2 display two-hybrid interactions with both wild-type and mutationally activated Cdc42 but not with a mutant version of Cdc42 that is predicted to be impaired in the ability to bind nucleotide, suggesting that Boi1 and Boi2 may associate with the GTP-bound ("active") form of Cdc42 [ 1 ] . Further evidence that some function of Boi1 is linked to that of Cdc42 is that overexpression of Boi1 inhibits bud emergence and that this inhibition can be suppressed by overexpression of Cdc42 [ 1 2 ] . RHO3 can serve as a multicopy suppressor of the lethality caused by deletion of BOI1 and BOI2 [ 1 2 ] . These findings are consistent with the possibilities that Boi1 and Boi2 are targets of Cdc42 that promote cell growth in a manner that is regulated by Rho3.
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