Determination of editors at the novel A-to-I editing positions

Nishimoto, Yoshinori; Yamashita, Takenari; Hideyama, Takuto; Tsuji, Shoji; Suzuki, Noriyuki; Kwak, Shin

doi:10.1016/j.neures.2008.02.009

Cited by 53 publications

(56 citation statements)

References 22 publications

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“…Using RNAi knockdown, we found that CYFIP2 mRNA had an ADAR2-mediated editing position and that BLCAP mRNA had an ADAR1-mediated editing position (Table 1) (36,37). In addition, we found that ADAR2 formed complexes with mRNAs with ADAR2-mediated editing positions including GluR2, kv1.1, and CYFIP2 mRNAs, particularly when the editing sites were edited in human cerebellum by means of the immunoprecipitation method.…”

Section: New Substrates Of Adar2mentioning

confidence: 84%

Novel Etiological and Therapeutic Strategies for Neurodiseases: RNA Editing Enzyme Abnormality in Sporadic Amyotrophic Lateral Sclerosis

et al. 2010

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Abstract. The motor neurons of patients with sporadic amyotrophic lateral sclerosis (ALS) express abundant Q/R site-unedited GluR2 mRNA, whereas those of patients with other motor neuron diseases including familial ALS associated with mutated SOD1 (ALS1) and those of normal subjects express only Q/R site-edited GluR2 mRNA. Because adenosine deaminase acting on RNA type 2 (ADAR2) specifically catalyzes GluR2 Q/R site-editing, it is likely that ADAR2 activity is not sufficient to edit this site completely in motor neurons of patients with sporadic ALS. Because these molecular abnormalities occur in disease-and motor neuron-specific fashion and induce fatal epilepsy in mice, we have hypothesized that GluR2 Q/R site-underediting due to ADAR2 underactivity is a cause of neuronal death in sporadic ALS. We found that cytoplasmic fragile X mental retardation protein interacting protein 2 (CYFIP2) mRNA had an ADAR2-mediated editing position using RNA interference knockdown. Our review will include a discussion of new ADAR2 substrates that may be useful for research on sporadic ALS.

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Section: New Substrates Of Adar2mentioning

confidence: 84%

Novel Etiological and Therapeutic Strategies for Neurodiseases: RNA Editing Enzyme Abnormality in Sporadic Amyotrophic Lateral Sclerosis

et al. 2010

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“…This strategy was demonstrated by a number of groups: looking for such conserved mismatches located in the exact same position in human and mouse resulted in a few additional A-to-I editing substrates. 24,26,27 The newly discovered sites are now under investigation in order to determine their biological function and regulation potential [28][29][30][31] . We note that using SPeciAL FocUS review review this approach one seems to be better off not implementing the requirement for a dsRNA structure, as the typical dsRNA structures of the few known targets are rather weak and hard to predict computationally.…”

Section: Bioinformatic Screensmentioning

confidence: 99%

Sequence based identification of RNA editing sites

Eisenberg¹,

Li²,

Levanon³

2010

RNA Biology

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“…The extent of CYFIP2 K/E site-editing are in the range of about 30% to 85% in the human brains and spinal cord. 10 Therefore, the extent of CYFIP2 K/E site-editing may become an additional marker for increase of GluR2-lacking Ca 2+ permeable AMPA receptors. Because GluR2 knockout mice did not display any neuronal death, 45 an increase of GluR2-lacking AMPA receptors per se cannot induce neuronal death and may be an exacerbating factor of excitotoxic neuronal death.…”

Section: A Tool For Sporadic Als Researchmentioning

confidence: 99%

“…An immunoprecipitation (IP) method and an in vitro RNAi knockdown system of ADAR1 and ADAR2 demonstrated that the K/E site in CYFIP2 mRNA and the Y/C site in BLCAP mRNA are edited predominantly by ADAR2 and ADAR1, respectively, and the Q/R site in FLNA mRNA is possibly edited by ADAR2. 10 In brief, CYFIP2, FLNA, GluR2 and kv1.1 mRNAs but not b-actin, BLCAP or IGFBP7 mRNA were recovered from an ADAR2-immunoprecipitate of the nuclear fraction of human cerebellum. Because GluR2 and kv1.1 mRNAs, but not b-actin mRNA, have ADAR2-mediated editing positions, these results suggest that CYFIP2 and FLNA mRNAs, but not BLCAP or IGFBP7 mRNA, have ADAR2-mediated positions.…”

mentioning

confidence: 92%