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Gene Review

RAB3GAP1  -  RAB3 GTPase activating protein subunit 1...

Homo sapiens

Synonyms: KIAA0066, P130, RAB3 GTPase-activating protein 130 kDa subunit, RAB3GAP, RAB3GAP130, ...
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Disease relevance of RAB3GAP1


High impact information on RAB3GAP1

  • Mutations of the catalytic subunit of RAB3GAP cause Warburg Micro syndrome [2].
  • Warburg Micro syndrome (WARBM1) is a severe autosomal recessive disorder characterized by developmental abnormalities of the eye and central nervous system and by microgenitalia [2].
  • We identified homozygous inactivating mutations in RAB3GAP, encoding RAB3 GTPase activating protein, a key regulator of the Rab3 pathway implicated in exocytic release of neurotransmitters and hormones, in 12 families with Micro syndrome [2].
  • We previously described inhibition of cell migration by PTEN and restoration of motility by focal adhesion kinase (FAK) and p130 Crk-associated substrate (p130(Cas)) [3].
  • We performed messenger RNA-expression studies of RAB3GAP1 and RAB3GAP2 orthologues in Danio rerio embryos and demonstrated that, whereas developmental expression of rab3gap1 was generalized (similar to that reported elsewhere in mice), rab3gap2 expression was restricted to the central nervous system [1].

Biological context of RAB3GAP1


Associations of RAB3GAP1 with chemical compounds

  • We propose that Rab3-GAP, like Ras- and Rho-GAPs, stabilizes the transition state of Rab3 and provides a critical arginine residue to accelerate the GTPase reaction [5].

Physical interactions of RAB3GAP1

  • Therefore, the Rab3-GAP-binding site involves the switch I region of Rab3 and overlaps with the Rabphilin-binding domain [5].

Other interactions of RAB3GAP1

  • Rab3 GEP stimulates the conversion of the GDP-bound inactive form to the GTP-bound active form, whereas Rab3 GAP stimulates the reverse reaction [6].
  • Furthermore, Rabphilin, a putative target of Rab3, inhibited the activity of Rab3-GAP on Rab3 [5].
  • CONCLUSION: These results indicate that rabconnectin-3 consists of the alpha and beta subunits and binds directly Rab3 GEP through the beta subunit and indirectly Rab3 GAP through an unidentified molecule(s) [7].

Analytical, diagnostic and therapeutic context of RAB3GAP1

  • By Western blot analysis with anti-MAP kinase antibodies, we demonstrate that p42 is one member of the mitogen-activating protein kinase, namely the p42MAPK [8].


  1. Mutation in Rab3 GTPase-activating protein (RAB3GAP) noncatalytic subunit in a kindred with Martsolf syndrome. Aligianis, I.A., Morgan, N.V., Mione, M., Johnson, C.A., Rosser, E., Hennekam, R.C., Adams, G., Trembath, R.C., Pilz, D.T., Stoodley, N., Moore, A.T., Wilson, S., Maher, E.R. Am. J. Hum. Genet. (2006) [Pubmed]
  2. Mutations of the catalytic subunit of RAB3GAP cause Warburg Micro syndrome. Aligianis, I.A., Johnson, C.A., Gissen, P., Chen, D., Hampshire, D., Hoffmann, K., Maina, E.N., Morgan, N.V., Tee, L., Morton, J., Ainsworth, J.R., Horn, D., Rosser, E., Cole, T.R., Stolte-Dijkstra, I., Fieggen, K., Clayton-Smith, J., Mégarbané, A., Shield, J.P., Newbury-Ecob, R., Dobyns, W.B., Graham, J.M., Kjaer, K.W., Warburg, M., Bond, J., Trembath, R.C., Harris, L.W., Takai, Y., Mundlos, S., Tannahill, D., Woods, C.G., Maher, E.R. Nat. Genet. (2005) [Pubmed]
  3. Shc and FAK differentially regulate cell motility and directionality modulated by PTEN. Gu, J., Tamura, M., Pankov, R., Danen, E.H., Takino, T., Matsumoto, K., Yamada, K.M. J. Cell Biol. (1999) [Pubmed]
  4. Platelet shape change induced by thrombin receptor activation. Rapid stimulation of tyrosine phosphorylation of novel protein substrates through an integrin- and Ca(2+)-independent mechanism. Negrescu, E.V., de Quintana, K.L., Siess, W. J. Biol. Chem. (1995) [Pubmed]
  5. Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP. Clabecq, A., Henry, J.P., Darchen, F. J. Biol. Chem. (2000) [Pubmed]
  6. Localization of the Rab3 small G protein regulators in nerve terminals and their involvement in Ca2+-dependent exocytosis. Oishi, H., Sasaki, T., Nagano, F., Ikeda, W., Ohya, T., Wada, M., Ide, N., Nakanishi, H., Takai, Y. J. Biol. Chem. (1998) [Pubmed]
  7. A novel rabconnectin-3-binding protein that directly binds a GDP/GTP exchange protein for Rab3A small G protein implicated in Ca(2+)-dependent exocytosis of neurotransmitter. Kawabe, H., Sakisaka, T., Yasumi, M., Shingai, T., Izumi, G., Nagano, F., Deguchi-Tawarada, M., Takeuchi, M., Nakanishi, H., Takai, Y. Genes Cells (2003) [Pubmed]
  8. Priming of tyrosine phosphorylation in GM-CSF-stimulated adherent neutrophils. Johnson, G.M., Gomez-Cambronero, J. J. Leukoc. Biol. (1995) [Pubmed]
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