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Gene Review

RasGAP1  -  Ras GTPase activating protein 1

Drosophila melanogaster

Synonyms: CG6721, Dmel\CG6721, GAP, GAP1, GTPase-activating protein, ...
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Disease relevance of Gap1


High impact information on Gap1

  • Inactivation of the locus, Gap1, mimics constitutive activation of the Sevenless receptor tyrosine kinase and eliminates the need for a functional Sevenless protein in the R7 cell [2].
  • The tumour-suppressor gene Neurofibromatosis 1 (Nf1) encodes a Ras-specific GTPase activating protein (Ras-GAP) [3].
  • In contrast, mutation of Y918, a site capable of binding mammalian rasGAP and PLC-gammal, increases Tor signaling [4].
  • Using this technique, we have identified a new mutant, mip (more inner photoreceptors), in which this map shows a striking hyperinnervation [5].
  • Cross GTPase-activating protein (CrossGAP)/Vilse links the Roundabout receptor to Rac to regulate midline repulsion [6].

Biological context of Gap1


Anatomical context of Gap1

  • Coimmunoprecipitation experiments in COS cells confirmed that HsAIRK-1 and HsAIRK-2 both interact with RasGAP [11].
  • RasGAP pull-down experiments showed that it interacts with HsAIRK-1 in G(2)/M HeLa cells [11].

Associations of Gap1 with chemical compounds

  • An inositol-1,3,4, 5-tetrakisphosphate (IP4)-sensitive extended PH domain is essential for Gap1 activity, while Ca2+-sensitive C2 domains and a glutamine-rich region contribute equally to full activity in vivo [8].
  • These results show that RasGAP can function as an inhibitor of signaling pathways mediated by Ras and receptor tyrosine kinases in vivo [1].
  • The interaction is dependent on the SH2 (Src homology 2) domains of RasGAP, which have been shown to interact with a phosphotyrosine residue within the consensus sequence (phospho)YXXPXD [12].
  • Identification of Aurora kinases as RasGAP Src homology 3 domain-binding proteins [11].

Other interactions of Gap1


Analytical, diagnostic and therapeutic context of Gap1

  • Sequence analysis revealed that the 2842-bp cDNA encodes a putative 628-amino acid protein product, which is a member of the GTPase-activating protein (GAP) family [15].


  1. Control of growth and differentiation by Drosophila RasGAP, a homolog of p120 Ras-GTPase-activating protein. Feldmann, P., Eicher, E.N., Leevers, S.J., Hafen, E., Hughes, D.A. Mol. Cell. Biol. (1999) [Pubmed]
  2. A putative Ras GTPase activating protein acts as a negative regulator of signaling by the Sevenless receptor tyrosine kinase. Gaul, U., Mardon, G., Rubin, G.M. Cell (1992) [Pubmed]
  3. A neurofibromatosis-1-regulated pathway is required for learning in Drosophila. Guo, H.F., Tong, J., Hannan, F., Luo, L., Zhong, Y. Nature (2000) [Pubmed]
  4. Drosophila terminal structure development is regulated by the compensatory activities of positive and negative phosphotyrosine signaling sites on the Torso RTK. Cleghon, V., Gayko, U., Copeland, T.D., Perkins, L.A., Perrimon, N., Morrison, D.K. Genes Dev. (1996) [Pubmed]
  5. mip causes hyperinnervation of a retinotopic map in Drosophila by excessive recruitment of R7 photoreceptor cells. Buckles, G.R., Smith, Z.D., Katz, F.N. Neuron (1992) [Pubmed]
  6. Cross GTPase-activating protein (CrossGAP)/Vilse links the Roundabout receptor to Rac to regulate midline repulsion. Hu, H., Li, M., Labrador, J.P., McEwen, J., Lai, E.C., Goodman, C.S., Bashaw, G.J. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  7. Ras1-mediated modulation of Drosophila homeotic function in cell and segment identity. Boube, M., Benassayag, C., Seroude, L., Cribbs, D.L. Genetics (1997) [Pubmed]
  8. In vivo functional analysis of Drosophila Gap1: involvement of Ca2+ and IP4 regulation. Powe, A.C., Strathdee, D., Cutforth, T., D'Souza-Correia, T., Gaines, P., Thackeray, J., Carlson, J., Gaul, U. Mech. Dev. (1999) [Pubmed]
  9. A novel mammalian Ras GTPase-activating protein which has phospholipid-binding and Btk homology regions. Maekawa, M., Li, S., Iwamatsu, A., Morishita, T., Yokota, K., Imai, Y., Kohsaka, S., Nakamura, S., Hattori, S. Mol. Cell. Biol. (1994) [Pubmed]
  10. Down-regulation of Drosophila Egf-r mRNA levels following hyperactivated receptor signaling. Sturtevant, M.A., O'Neill, J.W., Bier, E. Development (1994) [Pubmed]
  11. Identification of Aurora kinases as RasGAP Src homology 3 domain-binding proteins. Gigoux, V., L'Hoste, S., Raynaud, F., Camonis, J., Garbay, C. J. Biol. Chem. (2002) [Pubmed]
  12. p120 Ras GTPase-activating protein associates with fibroblast growth factor receptors in Drosophila. Woodcock, S.A., Hughes, D.A. Biochem. J. (2004) [Pubmed]
  13. Identification of chromosome inheritance modifiers in Drosophila melanogaster. Dobie, K.W., Kennedy, C.D., Velasco, V.M., McGrath, T.L., Weko, J., Patterson, R.W., Karpen, G.H. Genetics (2001) [Pubmed]
  14. Dynamic expression of d-CdGAPr, a novel Drosophila melanogaster gene encoding a GTPase activating protein. Sagnier, T., Grienenberger, A., Mariol, M., Bérenger, H., Pradel, J., Graba, Y. Mech. Dev. (2000) [Pubmed]
  15. Identification and characterization of a transcript for a novel Rac GTPase-activating protein in terminally differentiating 3T3-L1 adipocytes. Wooltorton, E.J., Haliotis, T., Mueller, C.R. DNA Cell Biol. (1999) [Pubmed]
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