Disease relevance of Rab2

• Expression levels of Rab2, a G protein, and Bag-1, a Bcl-2 binding protein are controlled by withdrawal of nicotine from cultured pheochromocytoma PC12 cells [1].

High impact information on Rab2

• Although GAPDH (C149G) has no catalytic activity, Rab2 recruited the mutant protein to membranes in a quantitative binding assay [2].
• Glyceraldehyde-3-phosphate dehydrogenase interacts with Rab2 and plays an essential role in endoplasmic reticulum to Golgi transport exclusive of its glycolytic activity [2].
• In contrast to Rab2, Rab2N'Delta19 failed to recruit PKCiota/lambda to normal rat kidney microsomes in a quantitative binding assay [3].
• Rab2 inhibited PKCiota/lambda-dependent GAPDH phosphorylation, whereas no effect was observed when the assay was performed with the aminoterminal truncation mutant [3].
• These combined results indicate that PKCiota/lambda is essential for protein transport in the early secretory pathway and suggest that PKCiota/lambda kinase activity is required to promote Rab2-mediated vesicle budding at a VTC subcompartment enriched in recycling cargo [4].

Biological context of Rab2

• Protein transport in the early secretory pathway requires Rab2 GTPase [5].
• The mutant protein binds GDP and GTP and has a low GTP hydrolysis rate that suggests that Rab2 Q65L is predominantly in the GTP-bound-activated form [6].

Anatomical context of Rab2

• Our previous work showed that Rab2 Q65L (equivalent to Ras Q61L) inhibited endoplasmic reticulum (ER)-to-Golgi transport in vivo [6].
• To complement the biochemical results, we observed in a morphological assay that Rab2 Q65L caused vesiculation of VTCs that accumulated at 15 degrees C. These data suggest that the Rab2 protein plays a role in the low-temperature-sensitive step that regulates membrane flow from VTCs to the Golgi complex and back to the ER [6].

Associations of Rab2 with chemical compounds

• The protein level of Rab2 was low in the presence of nicotine, but was rapidly increased after nicotine withdrawal [1].

Other interactions of Rab2

• We examined the changes in the protein levels of 2 GTP-binding proteins, Rab2 (Ras-related protein) and Rac1 [1].
• Purification and functional interactions of GRASP55 with Rab2 [7].
• Expression of anti-apoptotic genes, such as nucleophosmin/B23, Rab2, MAP kinase kinase and CREB binding protein, was up-regulated by dextromethorphan [8].

References