Evidence map›Paper›PMID 25266659›Full record

ArticleMolecular and cellular biology2014

CstF64: cell cycle regulation and functional role in 3' end processing of replication-dependent histone mRNAs.

Valentina Romeo, Esther Griesbach, Daniel Schümperli

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

30 citing papers in PubMed, 39 citations in OpenAlex.

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  20. Birth and Death of Histone mRNAs.Trends in genetics : TIG · 2017
    Review
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

3 authors at 1 institution in 1 country.

Valentina RomeoInstitute of Cell Biology, University of Bern, Bern, Switzerland Graduate School for Cellular and Biomedical Sciences, University of Bern, Bern, Switzerland.
Esther GriesbachInstitute of Cell Biology, University of Bern, Bern, Switzerland.
Daniel SchümperliInstitute of Cell Biology, University of Bern, Bern, Switzerland daniel.schuemperli@izb.unibe.ch.
University of Bern · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The 3' end processing of animal replication-dependent histone mRNAs is activated during G1/S-phase transition. The processing site is recognized by stem-loop binding protein and the U7 snRNP, but cleavage additionally requires a heat-labile factor (HLF), composed of cleavage/polyadenylation specificity factor, symplekin, and cleavage stimulation factor 64 (CstF64). Although HLF has been shown to be cell cycle regulated, the mechanism of this regulation is unknown. Here we show that levels of CstF64 increase toward the S phase and its depletion affects histone RNA processing, S-phase progression, and cell proliferation. Moreover, analyses of the interactions between CstF64, symplekin, and the U7 snRNP-associated proteins FLASH and Lsm11 indicate that CstF64 is important for recruiting HLF to histone precursor mRNA (pre-mRNA)-resident proteins. Thus, CstF64 is central to the function of HLF and appears to be at least partly responsible for its cell cycle regulation. Additionally, we show that misprocessed histone transcripts generated upon CstF64 depletion mainly accumulate in the nucleus, where they are targets of the exosome machinery, while a small cytoplasmic fraction is partly associated with polysomes.

Indexed as

Apoptosis Regulatory ProteinsCalcium-Binding ProteinsCell Line, TumorCell ProliferationCleavage And Polyadenylation Specificity FactorCleavage Stimulation FactorHEK293 CellsHeLa CellsHistonesHumansNuclear ProteinsRibonucleoprotein, U7 Small NuclearRNA 3' End ProcessingRNA-Binding ProteinsRNA PrecursorsS PhaseApoptosis Regulatory ProteinsCalcium-Binding ProteinsCASP8AP2 protein, humanCleavage And Polyadenylation Specificity FactorCleavage Stimulation FactorCSTF2T protein, humanHistonesLSM11 protein, humanNuclear ProteinsRibonucleoprotein, U7 Small NuclearRNA-Binding ProteinsRNA PrecursorsSYMPK protein, human

Identifiers

PMID25266659
PMCPMC4248742
OpenAlexW2151549812

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.