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Gene Review

Rab1a  -  RAB1A, member RAS oncogene family

Rattus norvegicus

Synonyms: Ac2-048, Rab1, Rab1A, Rab1r, Ras-related protein Rab-1A
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Disease relevance of Rab1

  • In the present study, we examine the role of guanine nucleotide dissociation inhibitor (GDI) in regulating the function of Rab1 in the transport of vesicular stomatitis virus glycoprotein (VSV-G) in vitro [1].

High impact information on Rab1

  • The mutant protein inhibits transfer of 3H-geranylgeranyl to wild-type Rab1A and Rab3A, suggesting that the enzyme recognizes conserved sequences distinct from the COOH-terminus [2].
  • Remarkably, DLP1-positive structures coalign with microtubules and, most strikingly, with endoplasmic reticulum tubules as verified by double labeling with antibodies to calnexin and Rab1 as well as by immunoelectron microscopy [3].
  • When the GDI-Rab1 complex was depleted from cytosol by use of a Rab1-specific antibody, VSV-G failed to exit the ER [1].
  • Guanine nucleotide dissociation inhibitor is essential for Rab1 function in budding from the endoplasmic reticulum and transport through the Golgi stack [1].
  • Incubation in the presence of excess GDI rapidly (t1/2 < 30 s) extracted Rab1 from membranes, inhibiting vesicle budding from the ER and sequential transport between the cis-, medial-, and trans-Golgi cisternae [1].

Biological context of Rab1

  • cDNA of a novel Ras-related GTP-binding protein was isolated from rat tissue by a PCR-based cloning approach, and was designated Rab29 because its deduced amino acid sequence (204 aa) is remotely similar to that of members of the Rab family (30% identity with Rab1). mRNA of Rab29 was found predominately in kidney [4].
  • A Rab1A effector domain peptide, Rab1AAL, and a scrambled peptide of Rab3AAL were less potent by several orders of magnitude in eliciting these responses compared with native Rab3 effector domain peptides [5].

Anatomical context of Rab1


Associations of Rab1 with chemical compounds

  • Following collapse of the Golgi into the ER in response to inhibition of activation of ARF1 by Brefeldin A, we found that Sar1- and Rab1-dependent Golgi reformation took place at multiple peripheral and perinuclear ER exit sites [8].

Regulatory relationships of Rab1


Other interactions of Rab1

  • The induction of such a GDI isoform at the beginning of the recovery stage correlates with the expression pattern of Rab1 and Rab5, but not Rab2 and Rab4 [10].

Analytical, diagnostic and therapeutic context of Rab1

  • Elevated expression of Rab1, the mammalian YPT1 homolog, protected against alphaSyn-induced dopaminergic neuron loss in animal models of PD [11].
  • Analysis of rat liver cytosol by gel filtration revealed that a major pool of Rab1 fractionates with a molecular mass of approximately 80 kD in the form of a GDI-Rab1 complex [1].


  1. Guanine nucleotide dissociation inhibitor is essential for Rab1 function in budding from the endoplasmic reticulum and transport through the Golgi stack. Peter, F., Nuoffer, C., Pind, S.N., Balch, W.E. J. Cell Biol. (1994) [Pubmed]
  2. Purification of component A of Rab geranylgeranyl transferase: possible identity with the choroideremia gene product. Seabra, M.C., Brown, M.S., Slaughter, C.A., Südhof, T.C., Goldstein, J.L. Cell (1992) [Pubmed]
  3. A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells. Yoon, Y., Pitts, K.R., Dahan, S., McNiven, M.A. J. Cell Biol. (1998) [Pubmed]
  4. Cloning of two splicing variants of the novel Ras-related GTPase Rab29 which is predominantly expressed in kidney. Massmann, S., Schürmann, A., Joost, H.G. Biochim. Biophys. Acta (1997) [Pubmed]
  5. Stimulation of inositol 1,4,5-trisphosphate production by peptides corresponding to the effector domain of different Rab3 isoforms and cross-linking of an effector domain peptide target. Piiper, A., Stryjek-Kaminska, D., Jahn, R., Zeuzem, S. Biochem. J. (1995) [Pubmed]
  6. On and off membrane dynamics of the endoplasmic reticulum-golgi tethering factor p115 in vivo. Brandon, E., Szul, T., Alvarez, C., Grabski, R., Benjamin, R., Kawai, R., Sztul, E. Mol. Biol. Cell (2006) [Pubmed]
  7. The carboxyl methyltransferase modifying G proteins is a metalloenzyme. Desrosiers, R.R., Nguyen, Q.T., Béliveau, R. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  8. The role of ARF1 and rab GTPases in polarization of the Golgi stack. Bannykh, S.I., Plutner, H., Matteson, J., Balch, W.E. Traffic (2005) [Pubmed]
  9. A Rab1 mutant affecting guanine nucleotide exchange promotes disassembly of the Golgi apparatus. Wilson, B.S., Nuoffer, C., Meinkoth, J.L., McCaffery, M., Feramisco, J.R., Balch, W.E., Farquhar, M.G. J. Cell Biol. (1994) [Pubmed]
  10. Differential expression pattern of Rab-GDI isoforms during the parotid gland secretion cycle. Benhar, M., Boschwitz, H., Linial, M. Exp. Cell Res. (1997) [Pubmed]
  11. Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Cooper, A.A., Gitler, A.D., Cashikar, A., Haynes, C.M., Hill, K.J., Bhullar, B., Liu, K., Xu, K., Strathearn, K.E., Liu, F., Cao, S., Caldwell, K.A., Caldwell, G.A., Marsischky, G., Kolodner, R.D., Labaer, J., Rochet, J.C., Bonini, N.M., Lindquist, S. Science (2006) [Pubmed]
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