Evidence map›Paper›PMID 37805921›Full record

ArticleCell reports2023

Splicing quality control mediated by DHX15 and its G-patch activator SUGP1.

Qing Feng, Keegan Krick, Jennifer Chu, Christopher B Burge

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 24 citations in OpenAlex.

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  13. Cancer-associated SF3B1 mutation K700E causes widespread changes in U2/branchpoint recognition without altering splicing.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

4 authors at 1 institution in 1 country.

Qing FengDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02138, USA. Electronic address: qfeng@mit.edu.
Keegan KrickDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02138, USA.
Jennifer ChuDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02138, USA.
Christopher B BurgeDepartment of Biology, Massachusetts Institute of Technology, Cambridge, MA 02138, USA. Electronic address: cburge@mit.edu.
Massachusetts Institute of Technology · US

Funding

VIRUS PRODUCTION COREP30CA014051 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI Paula T Hammond · 1985 to 2026
$93.9M
Regulation and Function of Alternative mRNA Isoform Expression in MammalsR01HG002439 · NHGRI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BURGE, CHRISTOPHER B · 2002 to 2024
$9.7M
Identification and Function of Sequence-specific Splicing RegulatorsR01GM085319 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BURGE, CHRISTOPHER B · 2008 to 2025
$5.2M
RNA-Binding Proteins as Molecular Integrators that Control the Response of HGSOC to Ant-Cancer TherapiesR01CA226898 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BURGE, CHRISTOPHER B, HEMANN, MICHAEL · 2019 to 2023
$2.7M
NCI NIH HHS P30 CA014051NCI NIH HHS R01 CA226898NHGRI NIH HHS R01 HG002439NIGMS NIH HHS R01 GM085319
6 · The paper itself

Abstract

Pre-mRNA splicing is surveilled at different stages by quality control (QC) mechanisms. The leukemia-associated DExH-box family helicase hDHX15/scPrp43 is known to disassemble spliceosomes after splicing. Here, using rapid protein depletion and analysis of nascent and mature RNA to enrich for direct effects, we identify a widespread splicing QC function for DHX15 in human cells, consistent with recent in vitro studies. We find that suboptimal introns with weak splice sites, multiple branch points, and cryptic introns are repressed by DHX15, suggesting a general role in promoting splicing fidelity. We identify SUGP1 as a G-patch factor that activates DHX15's splicing QC function. This interaction is dependent on both DHX15's ATPase activity and on SUGP1's U2AF ligand motif (ULM) domain. Together, our results support a model in which DHX15 plays a major role in splicing QC when recruited and activated by SUGP1.

Indexed as

RNA SplicingSpliceosomesHumansRNARNA HelicasesRNA PrecursorsRNA Splicing FactorsSplicing Factor U2AFDHX15 protein, humanRNARNA HelicasesRNA PrecursorsRNA Splicing FactorsSplicing Factor U2AFSUGP1 protein, humanCP: Molecular biologycryptic splicingG-patch domainneojunctionRNA helicasesplicing quality controlsplit APEXULM-UHM

Identifiers

PMID37805921
PMCPMC10842378
OpenAlexW4387439202

What OpenQuestion holds

Textmetadata
LicenceTDM
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.