Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity

@article{Gorvel1998DifferentialPO,
  title={Differential properties of D4/LyGDI versus RhoGDI: phosphorylation and rho GTPase selectivity},
  author={Jean Pierre Gorvel and T. C. T. Chang and Joelle Boretto and Takahiro Azuma and Philippe Chavrier},
  journal={FEBS Letters},
  year={1998},
  volume={422}
}
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TLDR
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TLDR
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TLDR
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TLDR
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Vav1 and Ly-GDI Two Regulators of Rho GTPases, Function Cooperatively as Signal Transducers in T Cell Antigen Receptor-induced Pathways*
TLDR
The data suggest that the interaction of Vav1 and Ly-GDI creates a fine tuning mechanism for the regulation of intracellular signaling pathways leading to NFAT stimulation.
Differential Localization of Rho Gtpases in Live Cells
TLDR
Despite the common essential feature of the CAAX (prenylation, AAX tripeptide proteolysis, and carboxyl methylation) motif, the subcellular localizations of Rho GTPases are diverse and dynamic.
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TLDR
Cell type-specific regulators of the Ras-like GTP-binding proteins may provide one mechanism by which different cell types respond uniquely to signals transduced through the same cell surface receptor or may provide a way by which the GTP -binding proteins can be uniquely engaged by tissue-restricted receptors.
Characterization of the Interaction between RhoGDI and Cdc42Hs Using Fluorescence Spectroscopy (*)
TLDR
The fluorescence assay for GDI interactions is used to demonstrate that the differences in functional potency observed between the GDI molecule and a related human leukemic protein, designated LD4, are due to differences in their binding affinities for Cdc42Hs.
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TLDR
GDI, by complexing with Rac‐GTP and preventing GAP stimulated GTP hydrolysis, may allow transit of the activated form of the Rac protein between physically separated activator and effector proteins in the cell.
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TLDR
Results suggest that R Ho GDI in the Rho A-Rho GDI complex is phosphorylated and that the stability of the complex depends on the phosphorylation state of Rho G DI.
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TLDR
It is shown that rho GDI regulates the binding of rhoB p20, a member of the rho gene products, to various membranes including rat brain synaptic plasma membranes and human erythrocyte ghosts.
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TLDR
It is found that RhoE in farnesylated in vivo and that this modification is required for association with the plasma membrane and with an unidentified cellular structure that may play a role in adhesion, suggesting a striking evolutionary divergence from the Rho family of GTPases.
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TLDR
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TLDR
Data on the cloning and structural analysis of the murine D4 cDNA is presented and it is suggested that D4, which will in subsequent communications be denoted as GDI, might be a GDI for other known or as yet unidentified ras‐like GTP‐binding proteins.
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