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Gene Review

Rab2a  -  RAB2A, member RAS oncogene family

Rattus norvegicus

Synonyms: Rab2, Ras-related protein Rab-2A
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Disease relevance of Rab2


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].


  1. 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. Yamada, K., Ishiguro, H., Ichino, N., Nishii, K., Sawada, H., Hida, T., Nagatsu, T. Journal of neural transmission (Vienna, Austria : 1996) (2005) [Pubmed]
  2. Glyceraldehyde-3-phosphate dehydrogenase interacts with Rab2 and plays an essential role in endoplasmic reticulum to Golgi transport exclusive of its glycolytic activity. Tisdale, E.J., Kelly, C., Artalejo, C.R. J. Biol. Chem. (2004) [Pubmed]
  3. Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation. Tisdale, E.J. J. Biol. Chem. (2003) [Pubmed]
  4. Atypical protein kinase C plays a critical role in protein transport from pre-Golgi intermediates. Tisdale, E.J., Wang, J., Silver, R.B., Artalejo, C.R. J. Biol. Chem. (2003) [Pubmed]
  5. Glyceraldehyde-3-phosphate dehydrogenase is required for vesicular transport in the early secretory pathway. Tisdale, E.J. J. Biol. Chem. (2001) [Pubmed]
  6. A Rab2 mutant with impaired GTPase activity stimulates vesicle formation from pre-Golgi intermediates. Tisdale, E.J. Mol. Biol. Cell (1999) [Pubmed]
  7. Purification and functional interactions of GRASP55 with Rab2. Barr, F.A. Meth. Enzymol. (2005) [Pubmed]
  8. Dextromethorphan alters gene expression in rat brain hippocampus and cortex. Lee, K.H., Ahn, J.I., Yu, D.H., Koh, H.C., Kim, S.H., Yang, B.H., Lee, Y.S., Lee, Y.S. Int. J. Mol. Med. (2003) [Pubmed]
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