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Arhgap35  -  Rho GTPase activating protein 35

Mus musculus

Synonyms: 6430596G11Rik, AI841135, Glucocorticoid receptor DNA-binding factor 1, Grlf1, Grlf1,Kiaa1722, ...
 
 
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Disease relevance of Grlf1

 

High impact information on Grlf1

  • p190 RhoGAP is a 190-kDa protein that stably associates with p120 RasGAP and regulates actin dynamics through members of the Rho family of small GTPases [4].
  • These results support the idea that Ras-GAP connects the Ras and Rho pathways and, therefore, regulates the actin cytoskeleton through a mechanism which probably does not involve p190 Rho-GAP [5].
  • Upon either direct activation of PKC or in response to integrin engagement, p190 RhoGAP is rapidly translocated to regions of membrane ruffling, where it colocalizes with polymerized actin [6].
  • Significantly, several of the observed tissue fusion defects seen in the mutant mice are also found in mice lacking MARCKS, the major substrate of protein kinase C (PKC), and we have found that p190 RhoGAP is also a PKC substrate in vivo [6].
  • Mice lacking functional p190 RhoGAP exhibit several defects in neural development that are reminiscent of those described in mice lacking certain mediators of neural cell adhesion [6].
 

Biological context of Grlf1

  • Our results suggest that p120-Gap has specific functions in downregulating the Ras/MAP kinase pathway following growth factor stimulation, and in modulating the phosphorylation of p190-rhoGap, but is not required for mitogenic signalling [7].
 

Anatomical context of Grlf1

 

Associations of Grlf1 with chemical compounds

  • Protein tyrosine phosphatase receptor type Z is involved in hippocampus-dependent memory formation through dephosphorylation at Y1105 on p190 RhoGAP [3].
 

Regulatory relationships of Grlf1

References

  1. p190 RhoGAP is the principal Src substrate in brain and regulates axon outgrowth, guidance and fasciculation. Brouns, M.R., Matheson, S.F., Settleman, J. Nat. Cell Biol. (2001) [Pubmed]
  2. Inactivation of Rho GTPases by p190 RhoGAP reduces human pancreatic cancer cell invasion and metastasis. Kusama, T., Mukai, M., Endo, H., Ishikawa, O., Tatsuta, M., Nakamura, H., Inoue, M. Cancer Sci. (2006) [Pubmed]
  3. Protein tyrosine phosphatase receptor type Z is involved in hippocampus-dependent memory formation through dephosphorylation at Y1105 on p190 RhoGAP. Tamura, H., Fukada, M., Fujikawa, A., Noda, M. Neurosci. Lett. (2006) [Pubmed]
  4. Phosphotyrosine (p-Tyr)-dependent and -independent mechanisms of p190 RhoGAP-p120 RasGAP interaction: Tyr 1105 of p190, a substrate for c-Src, is the sole p-Tyr mediator of complex formation. Roof, R.W., Haskell, M.D., Dukes, B.D., Sherman, N., Kinter, M., Parsons, S.J. Mol. Cell. Biol. (1998) [Pubmed]
  5. Ras-GAP controls Rho-mediated cytoskeletal reorganization through its SH3 domain. Leblanc, V., Tocque, B., Delumeau, I. Mol. Cell. Biol. (1998) [Pubmed]
  6. The adhesion signaling molecule p190 RhoGAP is required for morphogenetic processes in neural development. Brouns, M.R., Matheson, S.F., Hu, K.Q., Delalle, I., Caviness, V.S., Silver, J., Bronson, R.T., Settleman, J. Development (2000) [Pubmed]
  7. Aberrant Ras regulation and reduced p190 tyrosine phosphorylation in cells lacking p120-Gap. van der Geer, P., Henkemeyer, M., Jacks, T., Pawson, T. Mol. Cell. Biol. (1997) [Pubmed]
  8. p190 Rho-GTPase activating protein associates with plexins and it is required for semaphorin signalling. Barberis, D., Casazza, A., Sordella, R., Corso, S., Artigiani, S., Settleman, J., Comoglio, P.M., Tamagnone, L. J. Cell. Sci. (2005) [Pubmed]
  9. Oncogenic Ras leads to Rho activation by activating the mitogen-activated protein kinase pathway and decreasing Rho-GTPase-activating protein activity. Chen, J.C., Zhuang, S., Nguyen, T.H., Boss, G.R., Pilz, R.B. J. Biol. Chem. (2003) [Pubmed]
  10. Thy-1 regulates fibroblast focal adhesions, cytoskeletal organization and migration through modulation of p190 RhoGAP and Rho GTPase activity. Barker, T.H., Grenett, H.E., MacEwen, M.W., Tilden, S.G., Fuller, G.M., Settleman, J., Woods, A., Murphy-Ullrich, J., Hagood, J.S. Exp. Cell Res. (2004) [Pubmed]
  11. Rnd proteins function as RhoA antagonists by activating p190 RhoGAP. Wennerberg, K., Forget, M.A., Ellerbroek, S.M., Arthur, W.T., Burridge, K., Settleman, J., Der, C.J., Hansen, S.H. Curr. Biol. (2003) [Pubmed]
 
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