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RIC8A  -  RIC8 guanine nucleotide exchange factor A

Homo sapiens

Synonyms: Protein Ric-8A, Synembryn-A, synembryn, synembryn-A
 
 
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High impact information on RIC8A

  • The C-terminal region of RIC8A is homologous to subunit 6b of ubiquinol cytochrome c reductase (respiratory complex III), while the N-terminal region has intrinsic affinity for type II, but not for type I, tRNAs [1].
  • Knockdown of RIC8A in Leishmania lowered the mitochondrial content of type II tRNAs but raised that of type I tRNAs, with downstream effects on mitochondrial translation and respiration, and cell death [1].
  • Recent studies have led to the discovery of GPCR-independent activation of Galpha subunits by the guanine nucleotide exchange factor RIC-8 in both asymmetric cell division and synaptic vesicle priming in metazoan organisms [2].
  • Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein guanine nucleotide exchange factor [3].
  • Furthermore, synembryn was shown to translocate to the plasma membrane in response to carbachol and isoproterenol [4].
 

Associations of RIC8A with chemical compounds

 

Analytical, diagnostic and therapeutic context of RIC8A

  • Extending the study to other Galpha subunits, we found that Gqalpha also interacts with synembryn, and these interactions were confirmed by in vitro pull down studies and by in vivo confocal laser microscopy analysis [4].

References

  1. An RNA-binding respiratory component mediates import of type II tRNAs into Leishmania mitochondria. Chatterjee, S., Home, P., Mukherjee, S., Mahata, B., Goswami, S., Dhar, G., Adhya, S. J. Biol. Chem. (2006) [Pubmed]
  2. New roles for Galpha and RGS proteins: communication continues despite pulling sisters apart. Wilkie, T.M., Kinch, L. Curr. Biol. (2005) [Pubmed]
  3. Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein guanine nucleotide exchange factor. Tall, G.G., Krumins, A.M., Gilman, A.G. J. Biol. Chem. (2003) [Pubmed]
  4. Human brain synembryn interacts with Gsalpha and Gqalpha and is translocated to the plasma membrane in response to isoproterenol and carbachol. Klattenhoff, C., Montecino, M., Soto, X., Guzmán, L., Romo, X., García, M.A., Mellstrom, B., Naranjo, J.R., Hinrichs, M.V., Olate, J. J. Cell. Physiol. (2003) [Pubmed]
 
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