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

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

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

A-to-I RNA editing modifies a variety of biologically important mRNAs, and is specifically catalyzed by either adenosine deaminase acting on RNA type 1 (ADAR1) or type 2 (ADAR2) in mammals including human. Recently several novel A-to-I editing sites were identified in mRNAs abundantly expressed in mammalian organs by means of computational genomic analysis, but which enzyme catalyzes these editing sites has not been determined. Using RNA interference (RNAi) knockdowns, we found that cytoplasmic fragile X mental retardation protein interacting protein 2 (CYFIP2) mRNA had an ADAR2-mediated editing position and bladder cancer associated protein (BLCAP) mRNA had an ADAR1-mediated editing position. In addition, we found that ADAR2 forms a complex 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 immunoprecipitation (IP) method. CYFIP2 mRNA was ubiquitously expressed in human tissues with variable extents of K/E site editing. Because ADAR2 underactivity may be a causative molecular change of death of motor neurons in sporadic amyotrophic lateral sclerosis (ALS), this newly identified ADAR2-mediated editing position may become a useful tool for ALS research.

Original languageEnglish
Pages (from-to)201-206
Number of pages6
JournalNeuroscience Research
Volume61
Issue number2
DOIs
Publication statusPublished - 2008 Jun

Fingerprint

Messenger RNA
Adenosine Deaminase
Fragile X Mental Retardation Protein
RNA
RNA Editing
Amyotrophic Lateral Sclerosis
Motor Neurons
RNA Interference
Immunoprecipitation
Urinary Bladder Neoplasms
Cerebellum
Mammals
Proteins
Enzymes
Research

Keywords

  • Adenosine deaminase acting on RNA (ADAR)
  • Bladder cancer associated protein (BLCAP)
  • Cytoplasmic fragile X mental retardation protein interacting protein 2 (CYFIP2)
  • Immunoprecipitation (IP)
  • RNA editing
  • RNA interference (RNAi)

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Nishimoto, Y., Yamashita, T., Hideyama, T., Tsuji, S., Suzuki, N., & Kwak, S. (2008). Determination of editors at the novel A-to-I editing positions. Neuroscience Research, 61(2), 201-206. https://doi.org/10.1016/j.neures.2008.02.009

Determination of editors at the novel A-to-I editing positions. / Nishimoto, Yoshinori; Yamashita, Takenari; Hideyama, Takuto; Tsuji, Shoji; Suzuki, Norihiro; Kwak, Shin.

In: Neuroscience Research, Vol. 61, No. 2, 06.2008, p. 201-206.

Research output: Contribution to journalArticle

Nishimoto, Y, Yamashita, T, Hideyama, T, Tsuji, S, Suzuki, N & Kwak, S 2008, 'Determination of editors at the novel A-to-I editing positions', Neuroscience Research, vol. 61, no. 2, pp. 201-206. https://doi.org/10.1016/j.neures.2008.02.009
Nishimoto Y, Yamashita T, Hideyama T, Tsuji S, Suzuki N, Kwak S. Determination of editors at the novel A-to-I editing positions. Neuroscience Research. 2008 Jun;61(2):201-206. https://doi.org/10.1016/j.neures.2008.02.009
Nishimoto, Yoshinori ; Yamashita, Takenari ; Hideyama, Takuto ; Tsuji, Shoji ; Suzuki, Norihiro ; Kwak, Shin. / Determination of editors at the novel A-to-I editing positions. In: Neuroscience Research. 2008 ; Vol. 61, No. 2. pp. 201-206.
@article{a1831e5fa94346cd89fe0026c5476756,
title = "Determination of editors at the novel A-to-I editing positions",
abstract = "A-to-I RNA editing modifies a variety of biologically important mRNAs, and is specifically catalyzed by either adenosine deaminase acting on RNA type 1 (ADAR1) or type 2 (ADAR2) in mammals including human. Recently several novel A-to-I editing sites were identified in mRNAs abundantly expressed in mammalian organs by means of computational genomic analysis, but which enzyme catalyzes these editing sites has not been determined. Using RNA interference (RNAi) knockdowns, we found that cytoplasmic fragile X mental retardation protein interacting protein 2 (CYFIP2) mRNA had an ADAR2-mediated editing position and bladder cancer associated protein (BLCAP) mRNA had an ADAR1-mediated editing position. In addition, we found that ADAR2 forms a complex 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 immunoprecipitation (IP) method. CYFIP2 mRNA was ubiquitously expressed in human tissues with variable extents of K/E site editing. Because ADAR2 underactivity may be a causative molecular change of death of motor neurons in sporadic amyotrophic lateral sclerosis (ALS), this newly identified ADAR2-mediated editing position may become a useful tool for ALS research.",
keywords = "Adenosine deaminase acting on RNA (ADAR), Bladder cancer associated protein (BLCAP), Cytoplasmic fragile X mental retardation protein interacting protein 2 (CYFIP2), Immunoprecipitation (IP), RNA editing, RNA interference (RNAi)",
author = "Yoshinori Nishimoto and Takenari Yamashita and Takuto Hideyama and Shoji Tsuji and Norihiro Suzuki and Shin Kwak",
year = "2008",
month = "6",
doi = "10.1016/j.neures.2008.02.009",
language = "English",
volume = "61",
pages = "201--206",
journal = "Neuroscience Research",
issn = "0168-0102",
publisher = "Elsevier Ireland Ltd",
number = "2",

}

TY - JOUR

T1 - Determination of editors at the novel A-to-I editing positions

AU - Nishimoto, Yoshinori

AU - Yamashita, Takenari

AU - Hideyama, Takuto

AU - Tsuji, Shoji

AU - Suzuki, Norihiro

AU - Kwak, Shin

PY - 2008/6

Y1 - 2008/6

N2 - A-to-I RNA editing modifies a variety of biologically important mRNAs, and is specifically catalyzed by either adenosine deaminase acting on RNA type 1 (ADAR1) or type 2 (ADAR2) in mammals including human. Recently several novel A-to-I editing sites were identified in mRNAs abundantly expressed in mammalian organs by means of computational genomic analysis, but which enzyme catalyzes these editing sites has not been determined. Using RNA interference (RNAi) knockdowns, we found that cytoplasmic fragile X mental retardation protein interacting protein 2 (CYFIP2) mRNA had an ADAR2-mediated editing position and bladder cancer associated protein (BLCAP) mRNA had an ADAR1-mediated editing position. In addition, we found that ADAR2 forms a complex 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 immunoprecipitation (IP) method. CYFIP2 mRNA was ubiquitously expressed in human tissues with variable extents of K/E site editing. Because ADAR2 underactivity may be a causative molecular change of death of motor neurons in sporadic amyotrophic lateral sclerosis (ALS), this newly identified ADAR2-mediated editing position may become a useful tool for ALS research.

AB - A-to-I RNA editing modifies a variety of biologically important mRNAs, and is specifically catalyzed by either adenosine deaminase acting on RNA type 1 (ADAR1) or type 2 (ADAR2) in mammals including human. Recently several novel A-to-I editing sites were identified in mRNAs abundantly expressed in mammalian organs by means of computational genomic analysis, but which enzyme catalyzes these editing sites has not been determined. Using RNA interference (RNAi) knockdowns, we found that cytoplasmic fragile X mental retardation protein interacting protein 2 (CYFIP2) mRNA had an ADAR2-mediated editing position and bladder cancer associated protein (BLCAP) mRNA had an ADAR1-mediated editing position. In addition, we found that ADAR2 forms a complex 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 immunoprecipitation (IP) method. CYFIP2 mRNA was ubiquitously expressed in human tissues with variable extents of K/E site editing. Because ADAR2 underactivity may be a causative molecular change of death of motor neurons in sporadic amyotrophic lateral sclerosis (ALS), this newly identified ADAR2-mediated editing position may become a useful tool for ALS research.

KW - Adenosine deaminase acting on RNA (ADAR)

KW - Bladder cancer associated protein (BLCAP)

KW - Cytoplasmic fragile X mental retardation protein interacting protein 2 (CYFIP2)

KW - Immunoprecipitation (IP)

KW - RNA editing

KW - RNA interference (RNAi)

UR - http://www.scopus.com/inward/record.url?scp=42749096310&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=42749096310&partnerID=8YFLogxK

U2 - 10.1016/j.neures.2008.02.009

DO - 10.1016/j.neures.2008.02.009

M3 - Article

C2 - 18407364

AN - SCOPUS:42749096310

VL - 61

SP - 201

EP - 206

JO - Neuroscience Research

JF - Neuroscience Research

SN - 0168-0102

IS - 2

ER -