RASD Family, Member 2 Proteine (RASD2)

Human RASD Family, Member 2 (RASD2) Interaktionspartner

1. results support the hypothesis that Rhes expression is regulated by miRNA and indicate that miR-101 may be a potent modulator of Rhes expression in striatal neurons.

2. Study demonstrated that variation in the gene coding for RASD2 (rs6518956) affects in vivo prefrontal and striatal phenotypes in healthy human subjects that are relevant to schizophrenia

3. Rhes influences striatal cAMP/PKA-dependent signaling and synaptic plasticity in a gender-sensitive fashion

4. Findings reveal that ras homolog enriched in striatum is localized also in striatal cholinergic interneurons and, most importantly, lack of this G-protein, significantly alters dopamine D2 receptor modulation of striatal cholinergic excitability.

5. Rhes is reduced in the brains of Huntington's disease patients.

6. The findings of this study suggested that Rhes may play a crucial role in striatal iron homeostasis.

7. Rhes robustly binds the autophagy regulator Beclin-1, decreasing its inhibitory interaction with Bcl-2 independent of JNK-1 signaling.

8. The sequestering of Rhes through its binding to mutant huntingtin may decrease the ability of Rhes to perform vital physiological functions in the striatum neurons of Huntington disease patients. (Review)

9. Rhes is an imidazoline-regulated transcript in pancreatic beta-cells

10. Rhes can interfere with the functional activity of wt and mutated TSHr and with the respective hormone-stimulated cAMP production of FSHr and LHr.

11. The genes RASD2 might be vulnerability genes for neuropsychologically defined subgroups of schizophrenic patients.

12. The monomeric G proteins AGS1 and Rhes selectively influence Galphai-dependent signaling to modulate N-type (CaV2.2) calcium channels.

13. Binding to the Gbeta subunits involves the cationic regions of AGS1 and Rhes, and Data used Rhes-AGS1 chimeras to show that their different cationic regions determine the Gbeta-specificity of the interactions.

Mouse (Murine) RASD Family, Member 2 (RASD2) Interaktionspartner

1. guanine nucleotide exchange factor RasGRP1 inhibited Rhes-mediated control of striatal motor activity in mice. RasGRP1 stabilized Rhes, increasing its synaptic accumulation in the striatum.

2. that Rasd2 mutants display deficits in basal prepulse inhibition that, in turn, exacerbate gating disruption under psychotomimetic drug challenge

3. Study showed that both genetic deletion of Rhes and pharmacological blockade of mTORC1 significantly attenuate dyskinesia development by reducing the sensitization of striato-nigral medium-sized spiny neurons to levodopa

4. ectopic expression of Rhes in the cerebellum of N171-82Q mice, during the asymptomatic period led to an exacerbation of motor deficits, including loss of balance and motor incoordination with ataxia-like features

5. Rhes influences striatal cAMP/PKA-dependent signaling and synaptic plasticity in a gender-sensitive fashion

6. Brain Rhes expression is decreased in a mouse model of Huntington's disease.

7. Rhes robustly binds the autophagy regulator Beclin-1, decreasing its inhibitory interaction with Bcl-2 independent of JNK-1 signaling.

8. Rhes is necessary for Akt dephosphorylation by the striatal multi-protein complex

9. behavioral symptoms of HD are regulated by Rhes

10. This study demonstrated that Rhes-deleted mice are dramatically protected from neurotoxicity and motor dysfunction in a striatal-specific model of Huntington's disease elicited by 3-nitropropionic acid.

11. Ths results of this study indicted that Rhes physiologically binds to and activates mTOR in the striatum and L-DOPA-induced dyskinesia.

12. Rhes disruption affects selected behavioral competencies, including a gender-dependent increase in anxiety levels and a clear motor coordination deficit but no learning or memory impairment.

13. The absence of Rhes modulates cAMP/PKA signalling in both striatopallidal and striatonigral projection neurons by increasing Golf protein levels and, in turn, influencing motor responses challenged by dopaminergic agonist/antagonist.