Title : rab GTP-binding proteins with three different carboxyl-terminal cysteine motifs are modified in vivo by 20-carbon isoprenoids.

Pub. Date : 1992 Feb 25

PMID : 1740442






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 rab GTP-binding proteins with three different carboxyl-terminal cysteine motifs are modified in vivo by 20-carbon isoprenoids. Cysteine ArfGAP with FG repeats 1 Homo sapiens
2 rab GTP-binding proteins with three different carboxyl-terminal cysteine motifs are modified in vivo by 20-carbon isoprenoids. 20-carbon isoprenoids ArfGAP with FG repeats 1 Homo sapiens
3 When cellular isoprenoid synthesis is blocked by treatment of cells with lovastatin, rab proteins that are normally localized in membranes of the endoplasmic reticulum, Golgi apparatus, and endosomes accumulate in the cytosol. Terpenes ArfGAP with FG repeats 1 Homo sapiens
4 When cellular isoprenoid synthesis is blocked by treatment of cells with lovastatin, rab proteins that are normally localized in membranes of the endoplasmic reticulum, Golgi apparatus, and endosomes accumulate in the cytosol. Lovastatin ArfGAP with FG repeats 1 Homo sapiens
5 This change in rab protein localization is reversed by providing cells with mevalonate. Mevalonic Acid ArfGAP with FG repeats 1 Homo sapiens
6 These findings suggest that geranylgeranyl modification underlies the ability of rab GTP-binding proteins to associate with intracellular membranes, where they are postulated to function as mediators of vesicular traffic. geranylgeranyl ArfGAP with FG repeats 1 Homo sapiens