EC Number   |
General Information |
Reference |
|---|
   2.5.1.60 | malfunction |
Atrgtb2 disruption mutnt plants are indistinguishable from the wild-type plants in their morphology and the time of flowering. Both homozygous Atrgtb2 mutants produces normal siliques, phenotype, overview |
-, 738764 |
| 2.5.1.60 | malfunction |
homozygous mutants of the major beta-subunit of Arabidopsis enzyme (RGTB1) result in unprenylated RAB GTPase accumulation in the cytoplasm, up-regulation of several GTPases, endocytosis and exocytosis are downregulated, defects in shoot growth and morphogenesis, changed shoot gravitropism and reaction to etiolation |
710287 |
| 2.5.1.60 | malfunction |
overexpression of Rabs Rab5a, Rab7, and Rab27 is observed in various cancers, elevated levels of Rab25 in breast and ovarian cancer cells are reported to increase the aggressiveness of these cancers |
709461 |
| 2.5.1.60 | malfunction |
partial impairment in this enzyme activity in Arabidopsis, by disruption of the AtRGTB1 gene, is known to influence plant stature and disturb gravitropic and light responses. Mutations in each of the RGTB genes cause a tip growth defect, visible as root hair and pollen tube deformations. FM 1-43 styryl dye endocytosis and recycling are affected in the mutant root hairs. The double mutant, with both AtRGTB genes disrupted, is non-viable due to absolute male sterility. Doubly mutated pollen is shrunken, has an abnormal exine structure, and shows strong disorganization of internal membranes, particularly of the endoplasmic reticulum system. The self-infertility of the Atrgtb1 mutants is not due solely to disturbed flower development. Siliques of homozygous Atrgtb1 mutants are smaller and rarely contain any seeds, phenotype, overview |
-, 738764 |
| 2.5.1.60 | malfunction |
underprenylation of RabGTPases causes choroideremia, which is a rare genetic disease, affecting 4% of theblind population. It is due to mutation/lack of activity of the Rab escort protein,REP, while the activity of the Rab geranylgeranyl-transferase itself is not implicated, overview |
739491 |
| 2.5.1.60 | physiological function |
Arabidopsis RGTB1 and RGTB2 are biochemically redundant in vitro, suggesting that there might be additional factors that differentiate RGTB1 and RGTB2 functions in vivo. Alternatively, the partial redundancy of RGTB1 and RGTB2 in Arabidopsis may result from differential expression |
738686 |
| 2.5.1.60 | physiological function |
attachment of geranylgeranyl isoprenoids to Rab guanine triphosphatases, which are key regulators in vesicular transport |
709461 |
| 2.5.1.60 | physiological function |
cells from the gunmetal gm/gm mouse, which bear a homozygous mutation in protein geranylgeranyltransferase-II that results in about 80% reduced activity of this enzyme compared to wild-type or heterozygous mice, are more sensitive to the effects of active phosphonocarboxylates, including reducing macrophage cell viability, inhibiting osteoclast formation and inhibiting fluid-phase endocytosis |
721951 |
| 2.5.1.60 | physiological function |
GGTase3 consists of an orphan prenyltransferase alpha-subunit, PTAR1, and the catalytic beta-subunit of GGTase2, RabGGTB. GGTase3 geranylgeranylates FBXL2 to allow its localization at cell membranes, where the ubiquitin ligase mediates the polyubiquitylation of membrane-anchored proteins. In cells, FBXL2 is specifically recognized by GGTase3 despite having a typical C-terminal CaaX prenylation-motif that is predicted to be recognized by GGtase1 |
759843 |
| 2.5.1.60 | physiological function |
inhibition of GGTase II, but not GGTase I, leads to an increase in UPR and apoptosis markers. Inhibition produces a retention of mucin MUC1 protein inside the cell. Rab inhibition, via either GGDPS or GGTase II inhibition, results in cytotoxic effects across all tested cell lines |
759873 |
