Regulation of reversible binding of smg p25A, a ras p21-like GTP-binding protein, to synaptic plasma membranes and vesicles by its specific regulatory protein, GDP dissociation inhibitor.

Araki, Satoshi; Kikuchi, Akira; Hata, Yoshinobu; Isomura, Mitsuo; Takai, Yoshimi

doi:10.1016/s0021-9258(19)38260-2

Cited by 257 publications

(38 citation statements)

References 24 publications

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“…In the cell, many of the targets of the G proteins are in the membrane and G protein isoprenyl modification appears to mediate membrane binding. Cytosolic G proteins of the rho and rab families normally exist in the cell bound to their cognate GDIs, and the GDIs can actively remove their G proteins from the membrane [18][19][20]. This role of GDI in partitioning of the G proteins between membrane and cytosol may be physiologically more important than the inhibition of nucleotide dissociation.…”

Section: Introductionmentioning

confidence: 99%

A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm

et al. 1997

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The rhoGDI structure is notable for the existence of both a structured and a highly flexible domain, both of which appear to be required for the interaction with rac. The immunoglobulin-like fold of the structured domain is unusual for a cytoplasmic protein. The presence of equivalent cleavage sites in rhoGDI and the closely related D4/Ly-GDI (rhoGDI-2) suggest that proteolytic cleavage between the flexible and structured regions of rhoGDI may have a role in the regulation of the activity of members of this family. There is no detectable similarity between the structure of rhoGDI and the recently reported structure of rabGDI, which performs the same function as rhoGDI for the rab family of small G proteins.

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Section: Introductionmentioning

confidence: 99%

A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm

et al. 1997

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“…A model of the Rab functional mechanism has recently been proposed (2); in the cytosol, Rab proteins are found as complexes with a GDP dissociation inhibitor (GDI)1 protein (6)(7)(8)(9). Recent experiments have suggested that the GDI protein could deliver the Rab protein to a specific organelle (10,11).…”

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confidence: 99%

Two-hybrid System Screen with the Small GTP-binding Protein Rab6. IDENTIFICATION OF A NOVEL MOUSE GDP DISSOCIATION INHIBITOR ISOFORM AND TWO OTHER POTENTIAL PARTNERS OF Rab6

Janoueix‐Lerosey

Jollivet

Camonis

et al. 1995

Journal of Biological Chemistry

106

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Rab6 is a small GTP-binding protein that belongs to the Ras superfamily and is involved in intra-Golgi transport. Using a two-hybrid system screen of a mouse brain cDNA library, we have isolated several clones encoding proteins that interact with Rab6. Approximately 60% of the clones identified encoded a new mouse Rab GDP dissociation inhibitor (GDI) isoform. This GDI isoform is distinct from mouse mGDI-1 and mGDI-2, which have been characterized previously, and most likely represents the mouse counterpart of the rat Rab GDI beta isoform. In the two-hybrid system, GDI beta interacts with wild-type Rab6 and Rab5, but not with a GTP-bound Rab6 mutant, or a Rab6 mutant that cannot be post-translationally processed. We further examined whether mouse GDI beta is functional; we show that recombinant mouse GDI beta is able to remove several Rab proteins, including Rab1, Rab2, Rab4, and Rab6, from membranes. The identification of a third GDI isoform in mouse raised the question whether GDI genes belong to a larger multigenic family. We have shown, by Southern blot analysis of genomic DNA, that at least five GDI gene copies exist in both the mouse and rat genomes. In our two-hybrid screen, we have also characterized another clone that specifically interacts with Rab6. This clone was partially sequenced but shows no homology to known sequences. Finally, a third clone, interacting with both Rab5 and Rab6, also appears to encode a novel protein.

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“…In both cases, a continuous change in the membrane topology provokes the 'wave' that translocates the bolus. In support of this hypothesis, it is interesting that the rab proteins are found associated with membranes and in the cytoplasm (Araki et al, 1990;Fischer von Mollard et al, 1991). It is believed that during their physiological function they are recycled between these two pools, as is the case for coating proteins.…”

Section: Are Gtp-binding Proteins Involved In the Formation Of Macromolecular Complexes?mentioning

confidence: 90%

“…The models must include the participation of different regulatory or effector proteins that interact with rabs such as the GTPase activating proteins (GAPs) (Burstein et al, 1991), GDP dissociation stimulators (GDS) also named guanine nucleotide releasing factors (GRFs) (Burstein and Macara, 1992;Moya et al, 1993) and GDP dissociation inhibitors (GDIs) (Sasaki et al, 1991). These proteins are believed to regulate the activeinactive conformational states of rabs and, at least for rab3 GDI, the cycling of the protein between membranes and cytoplasm (Araki et al, 1990;Fischer von Mollard et al, 1991;Regazzi et al, 1992).…”

Section: The Mechanism Of Transport and The Gtp-binding Proteinsmentioning

confidence: 99%

Transport and internal organization of membranes: vesicles, membrane networks and GTP-binding proteins

Ayala

1994

Journal of Cell Science

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Eukaryotic cells contain a variety of membranous organelles such as the Golgi complex and endosomes, which are organized to allow the flow of molecules to specific regions within the cell. Well known examples of this targeted flow include the transport of specific molecules to the apical pole of epithelial cells, to the axon terminals of neurons, and the transcytosis of immunoglobulins. The generally accepted model of transport between the different intracellular compartments maintains that transport is mediated by carrier vesicles, but recent data show the participation of tubulovesicular structures in membrane transport, and the assumed discontinuity of some intracellular compartments has come under considerable scrutiny. It seems that for different intracellular pathways, eukaryotic cells use both the vesicular and the tubular (bolus) means of transport. In this article I will discuss the vesicular and the tubular models of transport as well as a hypothesis for the mechanism of action of small GTPases of the rab family in these movements.

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Regulation of reversible binding of smg p25A, a ras p21-like GTP-binding protein, to synaptic plasma membranes and vesicles by its specific regulatory protein, GDP dissociation inhibitor.

Cited by 257 publications

References 24 publications

A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm

A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm

Two-hybrid System Screen with the Small GTP-binding Protein Rab6. IDENTIFICATION OF A NOVEL MOUSE GDP DISSOCIATION INHIBITOR ISOFORM AND TWO OTHER POTENTIAL PARTNERS OF Rab6

Transport and internal organization of membranes: vesicles, membrane networks and GTP-binding proteins

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