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Gene Review

Ric  -  Ras-related protein interacting with...

Drosophila melanogaster

Synonyms: 17137290, CG8418, D-Ric, Dmel\CG8418, Q7JMZ0, ...
 
 
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High impact information on Ric

  • In a screen for calmodulin-binding proteins, we identified RIC, a protein related to the Ras subfamily of small GTPases [1].
  • In addition to the ability to bind calmodulin, a number of unique features distinguished RIC from other Ras-like GTPases, including the absence of a signal for prenylation and a distinct effector (G2) domain [1].
  • Unlike other Ras superfamily members, these proteins lack a signal for prenylation, contain a conserved but distinct effector domain, and, in the case of Rin and RIC, contain calmodulin-binding domains [2].
  • The mammalian Rit and Rin proteins, along with the Drosophila homologue RIC, comprise a distinct and evolutionarily conserved subfamily of Ras-related small GTP-binding proteins [2].
  • Expression of activated RIC proteins altered the development of well-characterized adult structures, including wing veins and photoreceptors of the compound eye [2].
 

Physical interactions of Ric

  • We conclude that the activation of the Ras cascade may be an important in vivo requisite to the transduction of signals through RIC and that the binding of calmodulin to RIC may negatively regulate this small GTPase [2].
 

Regulatory relationships of Ric

  • On the other hand, reduction of calmodulin exacerbated the defects caused by activated RIC, thus providing the first functional evidence for interaction of these molecules [2].

References

  1. RIC, a calmodulin-binding Ras-like GTPase. Wes, P.D., Yu, M., Montell, C. EMBO J. (1996) [Pubmed]
  2. Activated RIC, a small GTPase, genetically interacts with the Ras pathway and calmodulin during Drosophila development. Harrison, S.M., Rudolph, J.L., Spencer, M.L., Wes, P.D., Montell, C., Andres, D.A., Harrison, D.A. Dev. Dyn. (2005) [Pubmed]
 
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