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G3bp1  -  GTPase activating protein (SH3 domain)...

Mus musculus

Synonyms: AI849976, ATP-dependent DNA helicase VIII, B430204O07, C87777, G3BP-1, ...
 
 
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High impact information on G3bp

  • Both in mouse embryonic fibroblasts and during development, the absence of G3BP altered the expression of essential growth factors, among which imprinted gene products and growth arrest-specific mRNAs were outstanding [1].
  • Control of fetal growth and neonatal survival by the RasGAP-associated endoribonuclease G3BP [1].
  • The results demonstrate that G3BP is essential for proper embryonic growth and development by mediating the coordinate expression of multiple imprinted growth-regulatory transcripts [1].
  • G3BP-/- mice that survived to term exhibited increased apoptotic cell death in the central nervous system and neonatal lethality [1].
  • Mitogen activation of mRNA decay pathways likely involves specific endoribonucleases, such as G3BP, a phosphorylation-dependent endoribonuclease that associates with RasGAP in dividing but not quiescent cells [2].
 

Biological context of G3bp

  • The insulin-like growth factor mRNA binding-protein IMP-1 and the Ras-regulatory protein G3BP associate with tau mRNA and HuD protein in differentiated P19 neuronal cells [3].
  • Thus, a growth factor-induced change in mRNA decay may be modulated by the nuclear localization of a site-specific endoribonuclease such as G3BP [2].
 

Associations of G3bp with chemical compounds

  • G3BP exclusively cleaves between cytosine and adenine (CA) after a specific interaction with RNA through the carboxyl-terminal RRM-type RNA binding motif [2].
  • A G3BP mutant in which this serine is changed to alanine remains exclusively cytoplasmic, whereas a glutamate for serine substitution that mimics the charge of a phosphorylated serine is translocated to the nucleus [2].

References

  1. Control of fetal growth and neonatal survival by the RasGAP-associated endoribonuclease G3BP. Zekri, L., Chebli, K., Tourrière, H., Nielsen, F.C., Hansen, T.V., Rami, A., Tazi, J. Mol. Cell. Biol. (2005) [Pubmed]
  2. RasGAP-associated endoribonuclease G3Bp: selective RNA degradation and phosphorylation-dependent localization. Tourrière, H., Gallouzi, I.E., Chebli, K., Capony, J.P., Mouaikel, J., van der Geer, P., Tazi, J. Mol. Cell. Biol. (2001) [Pubmed]
  3. The insulin-like growth factor mRNA binding-protein IMP-1 and the Ras-regulatory protein G3BP associate with tau mRNA and HuD protein in differentiated P19 neuronal cells. Atlas, R., Behar, L., Elliott, E., Ginzburg, I. J. Neurochem. (2004) [Pubmed]
 
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