The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Rab4a  -  RAB4A, member RAS oncogene family

Rattus norvegicus

Synonyms: Rab4, Ras-related protein Rab-4A
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on Rab4a

  • Both Rab4 peptide and anti-Rab4 antibody enhanced calcium-stimulated amylase release from streptolysin O-permeabilized acini, suggesting the inhibitory role of Rab4 in exocytosis [1].
  • RESULTS: Rab4 was localized on zymogen granule membranes [1].
  • The participation of protein kinase C in the Rab4 regulation by CCK was confirmed by calphostin C pretreatment of acini [1].
  • The Rab4 function in regulated exocytosis was examined by introducing Rab4 hypervariable carboxy-terminal domain peptide (Rab4 peptide) and anti-Rab4 antibody into streptolysin O-permeabilized acini [1].
  • Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes [2].

Biological context of Rab4a

  • These findings suggested that Rab4 participates in endocytosis at the apical membrane of parotid glands [3].
  • Involvement of Rab4 in regulated exocytosis of rat pancreatic acini [1].
  • This hypothesis was strengthened by the fact that Rab4 deltaCT, a Rab4 mutant lacking the geranylgeranylation sites, inhibited insulin-induced recruitement of Glut4-myc to the cell surface, even when moderately overexpressed [2].
  • The purpose of this study was to determine if Rab4, a small GTP binding protein that has been implicated in the insulin-stimulated translocation of GLUT4 in adipose cells, is involved in the regulation of transporter translocation in skeletal muscle [4].

Anatomical context of Rab4a

  • Although alpha-adaptin was immunohistochemically distributed along the plasma membrane, this protein coexisted with Rab4 only at the apical region [3].
  • Membrane marker enzyme, 5' nucleotidase activity, and the early and recycling endosome markers Rab4 and Rab11 were used to verify the enrichment of these fractions [5].
  • Rab4 was localized mainly on the intracellular membranes in the subapical-actin terminal web, but was not present in the basolateral region both in acinar and ductal cells [3].
  • Detection of actin indicated that the Rab4-containing intracellular membranes were attached to the actin filaments [3].
  • Rab4 was redistributed to the cytosol and its movement was reversed by insulin withdrawal [6].

Associations of Rab4a with chemical compounds

  • A role for Rab4 in the translocation of the glucose transporter Glut4 induced by insulin has been recently proposed [2].
  • In the present study, we investigated the insulin effects on the guanine nucleotide exchange on Rab4 [7].
  • Guanine nucleotides exchanged into the Rab4 present on the vesicles as shown by solubilization of Rab4 by Rab-GDI; solubilization was inhibited by incubation with GTP-gamma-S and promoted by GDP [8].

Other interactions of Rab4a

  • Resensitization was minimally affected by inhibition of vacuolar H(+)-ATPase and phosphatases but was markedly suppressed by disruption of Rab4a and Rab11a [9].
  • 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].
  • These vesicles also containend Rab4 and Akt-2, the latter being only associated after insulin stimulation [11].
  • Western blot analysis demonstrated that the 27 kDa, 26 kDa, and 20 kDa proteins were Rab5p, Rab4p and ADP-ribosylation factor (ARF), respectively [12].

Analytical, diagnostic and therapeutic context of Rab4a


  1. Involvement of Rab4 in regulated exocytosis of rat pancreatic acini. Ohnishi, H., Mine, T., Shibata, H., Ueda, N., Tsuchida, T., Fujita, T. Gastroenterology (1999) [Pubmed]
  2. Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes. Cormont, M., Bortoluzzi, M.N., Gautier, N., Mari, M., van Obberghen, E., Le Marchand-Brustel, Y. Mol. Cell. Biol. (1996) [Pubmed]
  3. Co-localization of rab4 with endocytosis-related proteins in the rat parotid glands. Nashida, T., Yoshie, S., Imai, A., Shimomura, H. Arch. Histol. Cytol. (2003) [Pubmed]
  4. Differential effects of insulin and exercise on Rab4 distribution in rat skeletal muscle. Sherman, L.A., Hirshman, M.F., Cormont, M., Le Marchand-Brustel, Y., Goodyear, L.J. Endocrinology (1996) [Pubmed]
  5. Short-term stretch translocates the alpha-1-subunit of the Na pump to plasma membrane. Sevieux, N., Ark, M., Hornick, C., Songu-Mize, E. Cell Biochem. Biophys. (2003) [Pubmed]
  6. Insulin and okadaic acid induce Rab4 redistribution in adipocytes. Cormont, M., Tanti, J.F., Zahraoui, A., Van Obberghen, E., Tavitian, A., Le Marchand-Brustel, Y. J. Biol. Chem. (1993) [Pubmed]
  7. Insulin stimulates guanine nucleotide exchange on Rab4 via a wortmannin-sensitive signaling pathway in rat adipocytes. Shibata, H., Omata, W., Kojima, I. J. Biol. Chem. (1997) [Pubmed]
  8. Regulation of early endocytic vesicle motility and fission in a reconstituted system. Bananis, E., Murray, J.W., Stockert, R.J., Satir, P., Wolkoff, A.W. J. Cell. Sci. (2003) [Pubmed]
  9. Recycling and resensitization of the neurokinin 1 receptor. Influence of agonist concentration and Rab GTPases. Roosterman, D., Cottrell, G.S., Schmidlin, F., Steinhoff, M., Bunnett, N.W. J. Biol. Chem. (2004) [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. Rab11 is associated with GLUT4-containing vesicles and redistributes in response to insulin. Kessler, A., Tomas, E., Immler, D., Meyer, H.E., Zorzano, A., Eckel, J. Diabetologia (2000) [Pubmed]
  12. The small GTP-binding proteins Rab4 and ARF are associated with released exosomes during reticulocyte maturation. Vidal, M.J., Stahl, P.D. Eur. J. Cell Biol. (1993) [Pubmed]
WikiGenes - Universities