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Gene Review

Rab3a  -  RAB3A, member RAS oncogene family

Rattus norvegicus

Synonyms: Ras-related protein Rab-3A
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High impact information on Rab3a


Biological context of Rab3a


Anatomical context of Rab3a


Associations of Rab3a with chemical compounds

  • The association of GTP with the guanine nucleotide-free form of modified Rab3A is stimulated by the Rab3 GDP/GTP exchange protein (Rab3 GEP), and the dissociation of GTP from the GTP-bound form is markedly reduced by synaptic vesicle phospholipid [10].
  • The Rab3a-induced block in degranulation can be bypassed by stimulation of streptolysin-O-permeabilized cells with guanosine 5'-[gamma-thio]triphosphate [6].

Physical interactions of Rab3a

  • Furthermore, as it colocalized in most, but not all, structures with Rab3a, results support the hypothesis that rabphilin-3A is interacting with Rab3a [9].

Co-localisations of Rab3a


Regulatory relationships of Rab3a


Other interactions of Rab3a

  • While overexpression of Rab3a did not affect vesicle recycling, overexpression of Rab5a reduced the recycling pool size by 50% [5].
  • During differentiation, expression of the vesicular SNARE VAMP-2, the small GTP-binding protein Rab3a, and the target SNARE syntaxin-4 were up-regulated [12].
  • The pattern for accumulation of rabphilin-3A was similar to that of Rab3a accumulation, including the poor recycling [9].
  • It binds selectively to the GTP-bound form of Rab3a as well as of Rab3c [9].
  • Immunoreactivities of the synaptic vesicle-associated proteins Rab3a and SNAP25 were also observed in the cells [13].

Analytical, diagnostic and therapeutic context of Rab3a


  1. rSec6 and rSec8, mammalian homologs of yeast proteins essential for secretion. Ting, A.E., Hazuka, C.D., Hsu, S.C., Kirk, M.D., Bean, A.J., Scheller, R.H. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  2. Rim, a component of the presynaptic active zone and modulator of exocytosis, binds 14-3-3 through its N terminus. Sun, L., Bittner, M.A., Holz, R.W. J. Biol. Chem. (2003) [Pubmed]
  3. Comparison of the effects on secretion in chromaffin and PC12 cells of Rab3 family members and mutants. Evidence that inhibitory effects are independent of direct interaction with Rabphilin3. Chung, S.H., Joberty, G., Gelino, E.A., Macara, I.G., Holz, R.W. J. Biol. Chem. (1999) [Pubmed]
  4. The GTPase Rab3a is associated with large dense core vesicles in bovine chromaffin cells and rat PC12 cells. Darchen, F., Senyshyn, J., Brondyk, W.H., Taatjes, D.J., Holz, R.W., Henry, J.P., Denizot, J.P., Macara, I.G. J. Cell. Sci. (1995) [Pubmed]
  5. Real-time imaging of Rab3a and Rab5a reveals differential roles in presynaptic function. Star, E.N., Newton, A.J., Murthy, V.N. J. Physiol. (Lond.) (2005) [Pubmed]
  6. Rat basophilic leukaemia (RBL) cells overexpressing Rab3a have a reversible block in antigen-stimulated exocytosis. Smith, J., Thompson, N., Thompson, J., Armstrong, J., Hayes, B., Crofts, A., Squire, J., Teahan, C., Upton, L., Solari, R. Biochem. J. (1997) [Pubmed]
  7. Rab3a, a small GTP-binding protein, undergoes fast anterograde transport but not retrograde transport in neurons. Li, J.Y., Jahn, R., Dahlström, A. Eur. J. Cell Biol. (1995) [Pubmed]
  8. Differential expression of Rab3 isoforms in high- and low-secreting mast cell lines. Carroll, K., Ray, K., Helm, B., Carey, E. Eur. J. Cell Biol. (2001) [Pubmed]
  9. Rabphilin-3A is transported with fast anterograde axonal transport and associated with synaptic vesicles. Li, J.Y. Synapse (1996) [Pubmed]
  10. A novel function of the C-terminal lipid moieties of Rab3A small G protein implicated in Ca2+-dependent exocytosis--inhibition of interaction with GTP and reduction of this inhibition by phospholipid. Jin-no, Y., Shirataki, H., Senbonmatsu, T., Yamamoto, T., Fujita, Y., Nakanishi, H., Takai, Y. Genes Cells (1997) [Pubmed]
  11. Distribution of Rab3a in rat nervous system: comparison with other synaptic vesicle proteins and neuropeptides. Li, J.Y., Jahn, R., Hou, X.E., Kling-Petersen, A., Dahlström, A. Brain Res. (1996) [Pubmed]
  12. SNARE complex proteins, including the cognate pair VAMP-2 and syntaxin-4, are expressed in cultured oligodendrocytes. Madison, D.L., Krueger, W.H., Cheng, D., Trapp, B.D., Pfeiffer, S.E. J. Neurochem. (1999) [Pubmed]
  13. Synaptic vesicle proteins in cells of the sympathoadrenal lineage. Hou, X.E., Dahlström, A. J. Auton. Nerv. Syst. (1996) [Pubmed]
  14. Double in situ hybridization reveals overlapping neuronal populations expressing the low molecular weight GTPases Rab3a and Rab3b in Rat brain. Stettler, O., Nothias, F., Tavitian, B., Vernier, P. Eur. J. Neurosci. (1995) [Pubmed]
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