Evidence map›Paper›PMID 29390077›Full record

ArticleNucleic acids research2018

Cwc23 is a component of the NTR complex and functions to stabilize Ntr1 and facilitate disassembly of spliceosome intermediates.

Yu-Lun Su, Hsin-Chou Chen, Rong-Tzong Tsai, Pei-Chun Lin, Soo-Chen Cheng

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Arresting Spliceosome Intermediates at Various Stages of the Splicing Pathway.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  4. Review
  5. Article
  6. Article
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

5 authors at 1 institution in 1 country.

Yu-Lun SuInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 115, Republic of China.
Hsin-Chou ChenInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 115, Republic of China.
Rong-Tzong TsaiInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 115, Republic of China.
Pei-Chun LinInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 115, Republic of China.
Soo-Chen ChengInstitute of Molecular Biology, Academia Sinica, Taipei, Taiwan 115, Republic of China.
Institute of Molecular Biology, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cwc23 is a member of the J protein family, and has been shown to interact with Ntr1, a scaffold protein that interacts with Ntr2 and Prp43 to form the NTR complex that mediates spliceosome disassembly. We show that Cwc23 is also an intrinsic component of the NTR complex, and that it interacts with the carboxyl terminus of Ntr1. Metabolic depletion of Cwc23 concurrently depleted Ntr1 and Ntr2, suggesting a role for Cwc23 in stabilizing these two proteins. Ntr1, Ntr2 and Cwc23 are stoichiometrically balanced, and form a stable heterotrimer. Depletion of Cwc23 from splicing extracts using antibodies resulted in depletion of all three proteins and accumulation of intron-lariat in the splicing reaction. Cwc23 is not required for disassembly of intron-lariat spliceosome (ILS), but facilitates disassembly of spliceosome intermediates after the actions of Prp2 and Prp16 by stabilizing the association of Ntr1 with the spliceosome. Cwc23 has a more limited effect on the association of Ntr1 with the ILS. Our data suggest that Cwc23 is important for maintaining the levels of Ntr1 and Ntr2, and that it also plays a regulatory role in targeting spliceosome intermediates for disassembly.

Indexed as

Adenosine TriphosphatasesDEAD-box RNA HelicasesIntronsMolecular ChaperonesProtein BindingRNA HelicasesRNA SplicingRNA Splicing FactorsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpliceosomesAdenosine TriphosphatasesCwc23 protein, S cerevisiaeDEAD-box RNA HelicasesMolecular ChaperonesNtr2 protein, S cerevisiaePRP16 protein, S cerevisiaePRP2 protein, S cerevisiaeRNA HelicasesRNA Splicing FactorsSaccharomyces cerevisiae ProteinsSpp382 protein, S cerevisiae

Identifiers

PMID29390077
PMCPMC6044358
OpenAlexW2792777454

What OpenQuestion holds

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LicenceCC BY-NC
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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.