Evidence map›Paper›PMID 29168419›Full record

ArticleRNA biology2018

Truncated forms of U2 snRNA (U2-tfs) are shunted toward a novel uridylylation pathway that differs from the degradation pathway for U1-tfs.

Hideaki Ishikawa, Yuko Nobe, Keiichi Izumikawa, Masato Taoka, Yoshio Yamauchi, Hiroshi Nakayama, Richard J Simpson, Toshiaki Isobe, Nobuhiro Takahash

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.7field-weighted citation impact, top 30% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 12 citations in OpenAlex.

  1. DIS3L2-mediated RNA surveillance and extracellular vesicle packaging prevent innate immune activation by aberrant cellular RNAs.Proceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 4 institutions in 2 countries.

Hideaki Ishikawaa Department of Applied Biological Science , Graduate School of Agriculture, Tokyo University of Agriculture and Technology , Fuchu-shi, Tokyo , Japan.
Yuko Nobec Department of Chemistry , Graduate School of Sciences and Engineering, Tokyo Metropolitan University , Hachiouji-shi, Tokyo , Japan.ORCID 0000-0001-6375-983X
Keiichi Izumikawaa Department of Applied Biological Science , Graduate School of Agriculture, Tokyo University of Agriculture and Technology , Fuchu-shi, Tokyo , Japan.
Masato Taokac Department of Chemistry , Graduate School of Sciences and Engineering, Tokyo Metropolitan University , Hachiouji-shi, Tokyo , Japan.
Yoshio Yamauchic Department of Chemistry , Graduate School of Sciences and Engineering, Tokyo Metropolitan University , Hachiouji-shi, Tokyo , Japan.
Hiroshi Nakayamad Biomolecular Characterization Unit , RIKEN Center for Sustainable Resource Science , Wako , Saitama , Japan.
Richard J Simpsonb Global Innovation Research Organization , Tokyo University of Agriculture and Technology , Fuchu-Shi, Tokyo , Japan.
Toshiaki Isobec Department of Chemistry , Graduate School of Sciences and Engineering, Tokyo Metropolitan University , Hachiouji-shi, Tokyo , Japan.
Nobuhiro Takahasha Department of Applied Biological Science , Graduate School of Agriculture, Tokyo University of Agriculture and Technology , Fuchu-shi, Tokyo , Japan.
Tokyo Metropolitan University · JPTokyo University of Agriculture and Technology · JPLa Trobe University · AURIKEN Center for Sustainable Resource Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

During the biogenesis of U1 small nuclear ribonucleoprotein, a small population of U1 snRNA molecules acquires an extra methylation at the first transcribed nucleotide and a nucleolytic cleavage to remove the 3' structured region including the Sm protein-binding site and stem-loop 4. These modifications occur before hypermethylation of the monomethylated 5' cap, whereby producing truncated forms of U1 snRNA (U1-tfs) that are diverted from the normal pathway to a processing body-associated degradation pathway. Here, we demonstrate that a small population of U2 snRNA molecules receives post-transcriptional modifications similar to those of U1 to yield U2-tfs. Like U1-tfs, U2-tfs molecules were produced from transcripts of the U2 snRNA gene having all cis-elements or lacking the 3' box. Unlike U1-tfs, however, a portion of U2-tfs received additional uridylylation of up to 5 nucleotides in length at position 87 (designated as U2-tfs-polyU) and formed an Sm protein-binding site-like structure that was stabilized by the small nuclear ribonucleoprotein SmB/B' probably as a part of heptameric Sm core complex that associates to the RNA. Both U2-tfs and U2-tfs-polyU were degraded by a nuclease distinct from the canonical Dis3L2 by a process catalyzed by terminal uridylyltransferase 7. Collectively, our data suggest that U2 snRNA biogenesis is regulated, at least in part, by a novel degradation pathway to ensure that defective U2 molecules are not incorporated into the spliceosome.

Indexed as

Cell LineHumansModels, MolecularNucleic Acid ConformationRibonucleoproteins, Small NuclearRNA Processing, Post-TranscriptionalRNA, Small NuclearRibonucleoproteins, Small NuclearRNA, Small NuclearU2 small nuclear RNARNA processingRNA surveillancesnRNP biogenesisspliceosomesplicingterminal uridylyltransferase 7uridine-rich small nuclear RNAuridylylation

Identifiers

PMID29168419
PMCPMC5798949
OpenAlexW2770318073

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.