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geranylgeranyl diphosphate + Arabidopsis thaliana RAB-ATa protein
S-geranylgeranyl-RAB GTPase + diphosphate
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homozygous insertion mutants (rgtb1-1 and rgtb1-2) of the major beta-subunit of Arabidopsis enzyme (RGTB1) lead to reduced enzyme activity (about 25%), 50 mM phosphate buffer, pH 7.6, 10 mM MgCl2, 5 mM DTT, 0.5 microM tritium-labelled all trans-geranylgeranyl pyrophosphate, 4 microg recombinant Arabidopsis thaliana RAB-A2a protein, 32°C, 40 min
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geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
geranylgeranyl diphosphate + Rab
S-geranylgeranyl-Rab + diphosphate
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His6- and gluthathione S-transferase-tagged Rab proteins such as canine Rab1a, human Rab27a, Rab5a, Rab18, Rab6a, Rab13, and mouse Rab23
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geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
additional information
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geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
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the Rab protein Rab8-GTPase, which end with a Cys-Val-Leu-Leu motif able to serve as a substrate for either geranylgeranyl transferase I and II, but modified predominantly by either geranylgeranyl transferase II in vivo
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geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
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reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins
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geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
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the enzyme catalyzes posttranslational modification of proteins, the farnesyl moieties attached to the substrates are directly involved in protein-protein interactions as well as in protein-membrane interactions
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geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
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enzyme crucial for membrane association and function of Rab proteins in intracellular vesicular trafficking
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geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
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reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins
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geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
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this posttranslational modification is essential for the biological activity of Rab proteins
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geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
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enzyme crucial for membrane association and function of Rab proteins in intracellular vesicular trafficking
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geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
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geranylgeranyl diphosphate + protein-cysteine
S-geranylgeranyl-protein + diphosphate
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reaction is critical for membrane localization of Rab proteins and for their interaction with soluble regulatory proteins
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geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
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intracellular vesicular trafficking is regulated by Rab proteins, small GTPases that require posttranslational geranylgeranylation for biological activity, which is catalyzed by the enzyme, a Rab geranylgeranyl transferase in complex with the Rab escort protein, REP, overview
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geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
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intracellular vesicular trafficking is regulated by Rab proteins, small GTPases that require posttranslational geranylgeranylation for biological activity, which is catalyzed by the enzyme, a Rab geranylgeranyl transferase together with the Rab escort protein, REP, overview
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geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
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geranylgeranyl diphosphate + Rab protein
S-geranylgeranyl-Rab protein + diphosphate
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Rab proteins are members of the Ras superfamily of GTPases and are key regulators of intracellular vesicular transport, they undergo a cycle of GTPase activity, and this activity is interconnected to a cycle of reversible attachment to membranes. This cycle is mediated by geranylgeranylation of usually two C-terminal cysteines, which in turn is effected by Rab geranylgeranyltransferase in concert with Rab escort protein REP, Rab prenylation, delivery to membranes and the GTPase cycle, overview, alternative and classical pathways, overview
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additional information
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reduction in RabGGT function can be sufficient to induce cancer cell lines to undergo p53-independent apoptosis
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additional information
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reduction in RabGGT function can be sufficient to induce cancer cell lines to undergo p53-independent apoptosis
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additional information
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unlike the other prenyltransferases, farnesyl-transferase and geranylgeranyl-transferase I (GGTaseI), RabGGTase does not rely on a consensus sequence such as the CAAX box, but instead has delegated substrate recognition to a third protein, the Rab escort protein (REP)
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additional information
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RabGGTase, which prenylates more than 60 members of the Rab GTPase family, can act on its protein substrates only when they are complexed to an additional factor termed REP, Rab escort protein
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additional information
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structural and mechanistic basis for recycling of Rab proteins between membrane compartments, overview
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