PKA modulates iron trafficking in the striatum via small GTPase, Rhes

B. R. Choi, S. Bang, Y. Chen, J. H. Cheah, S. F. Kim

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


Ras homolog enriched in striatum (Rhes), is a highly conserved small guanosine-5'-triphosphate (GTP) binding protein belonging to the Ras superfamily. Rhes is involved in the dopamine receptor-mediated signaling and behavior though adenylyl cyclase. The striatum-specific GTPase share a close homology with Dexras1, which regulates iron trafficking in the neurons when activated though the post-translational modification called s-nitrosylation by nitric oxide (NO). We report that Rhes physiologically interacted with Peripheral benzodiazepine receptor-associated protein7 and participated in iron uptake via divalent metal transporter 1 similar to Dexras1. Interestingly, Rhes is not S-nitrosylated by NO-treatment, however phosphorylated by protein kinase A at the site of serine-239. Two Rhes mutants - the phosphomimetic form (serine 239 to aspartic acid) and constitutively active form (alanine 173 to valine) - displayed an increase in iron uptake compared to the wild-type Rhes. These findings suggest that Rhes may play a crucial role in striatal iron homeostasis.

Original languageEnglish (US)
Pages (from-to)214-220
Number of pages7
StatePublished - Dec 3 2013
Externally publishedYes


  • G protein
  • Iron uptake
  • PKA
  • Phosphorylation
  • Rhes
  • Striatum

ASJC Scopus subject areas

  • Neuroscience(all)


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