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Gene Review

ARHGAP29  -  Rho GTPase activating protein 29

Homo sapiens

Synonyms: PARG1, PTPL1-associated RhoGAP protein 1, Rho GTPase-activating protein 29, Rho-type GTPase-activating protein 29
 
 
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High impact information on ARHGAP29

  • In this review, we highlight current areas of investigation such as the clinical potential of PARP and PARG inhibitors and the important mitotic regulatory functions of poly(ADP-ribose) in cell-cycle progression, a recent discovery that has broadened our knowledge regarding poly(ADP-ribose) functions [1].
  • PARG1 interacted with Rap2 in a GTP-dependent manner but not with Ras or Rap1 [2].
  • To overcome the early embryonic lethality of parg-knockout mice and gain more insights into the biological functions of PARG, we used an RNA interference approach [3].
  • Inclusion of tryptophan in plys and parg diminished their effect, whereas inclusion of serine in plys,ser (3:1) improved it [4].
  • Polymers of lys (plys) and arg (parg) were found to be efficient inhibitors of the formation of complexes between low density lipoprotein (LDL) and human chondroitin-6-sulfate-rich proteoglycans [4].
 

Associations of ARHGAP29 with chemical compounds

  • Poly-L-lys (plys) and poly-L-arg (parg) exhibited similar displacing ability [4].
 

Regulatory relationships of ARHGAP29

 

Other interactions of ARHGAP29

  • Here we show that the ZPH region of PARG1 mediates interaction with Rap2 [2].

References

  1. The expanding role of poly(ADP-ribose) metabolism: current challenges and new perspectives. Gagné, J.P., Hendzel, M.J., Droit, A., Poirier, G.G. Curr. Opin. Cell Biol. (2006) [Pubmed]
  2. PARG1, a protein-tyrosine phosphatase-associated RhoGAP, as a putative Rap2 effector. Myagmar, B.E., Umikawa, M., Asato, T., Taira, K., Oshiro, M., Hino, A., Takei, K., Uezato, H., Kariya, K. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  3. Poly(ADP-ribose) glycohydrolase silencing protects against H2O2-induced cell death. Blenn, C., Althaus, F.R., Malanga, M. Biochem. J. (2006) [Pubmed]
  4. Cationic polypeptides modulate in vitro association of low density lipoprotein with arterial proteoglycans, fibroblasts, and arterial tissue. Wiklund, O., Camejo, G., Mattsson, L., Lopez, F., Bondjers, G. Arteriosclerosis (1990) [Pubmed]
 
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