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Gene Review

Rab6a  -  RAB6A, member RAS oncogene family

Rattus norvegicus

Synonyms: RCO4-3, Rab-6, Rab6, Rab6b, Ras-related protein Rab-6A
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High impact information on Rab6a

  • Our observations support the role of a prenylated protein, such as the geranylgeranylated small G protein Rab6, in the retrograde transport from the Golgi apparatus to the ER, since lovastatin acts by inhibiting its prenylation [1].
  • In rat AR4-2J cells, Rab6 as well as Rab1A/B and Rab2, partitioned between the cytosol and microsomes [2].
  • Because Rab6 is involved in vesicle transport in the Golgi apparatus and the trans-Golgi network, we confirmed the presence of Rab6 in these cells [2].
  • Immunoblotting showed that ethanol induced a transient reduction in Rab6 after 5 days of ethanol exposure, whereas Rab3B decreased after 20 days, Rab11 after 30 days, and Rab1B after 60 days [3].
  • Because small GTP-binding proteins of Rab family have been implicated as key regulators of membrane and protein trafficking in mammalian cells, this study was designed to test if ethanol-impaired pituitary FSH and LH secretion is associated with changes in Rab proteins, particularly Rab1B, Rab3B, Rab6, and Rab11 [3].

Anatomical context of Rab6a


Analytical, diagnostic and therapeutic context of Rab6a


  1. Functional protein prenylation is required for the brefeldin A-dependent retrograde transport from the Golgi apparatus to the endoplasmic reticulum. Ivessa, N.E., Gravotta, D., De Lemos-Chiarandini, C., Kreibich, G. J. Biol. Chem. (1997) [Pubmed]
  2. Impairment of bile salt-dependent lipase secretion in human pancreatic tumoral SOJ-6 cells. Caillol, N., Pasqualini, E., Lloubes, R., Lombardo, D. J. Cell. Biochem. (2000) [Pubmed]
  3. Ethanol-induced alterations in Rab proteins: possible implications for pituitary dysfunction. Ren, J.C., Zhu, Q., Lapaglia, N., Emanuele, N.V., Emanuele, M.A. Alcohol (2005) [Pubmed]
  4. Small GTP-binding protein, Rab6, is associated with secretory granules in atrial myocytes. Iida, H., Tanaka, S., Shibata, Y. Am. J. Physiol. (1997) [Pubmed]
  5. Organellar proteomics: analysis of pancreatic zymogen granule membranes. Chen, X., Walker, A.K., Strahler, J.R., Simon, E.S., Tomanicek-Volk, S.L., Nelson, B.B., Hurley, M.C., Ernst, S.A., Williams, J.A., Andrews, P.C. Mol. Cell Proteomics (2006) [Pubmed]
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