Evidence map›Paper›PMID 38182103›Full record

ArticleJournal of molecular biology2024

KH-like Domains in PARP9/DTX3L and PARP14 Coordinate Protein-Protein Interactions to Promote Cancer Cell Survival.

Hadil Saleh, Triantafillos Liloglou, Daniel J Rigden, Jason L Parsons, Gabrielle J Grundy

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.8field-weighted citation impact, top 2% 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

19 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
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  3. Oncology research · 2026
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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

5 authors at 3 institutions in 1 country.

Hadil SalehUniversity of Liverpool, Department of Molecular and Clinical Cancer Medicine, 6 West Derby St, Liverpool L7 8TX, UK.
Triantafillos LiloglouEdge Hill University, Faculty of Health, Social Care & Medicine, St Helens Road, Ormskirk, Lancashire L39 4QP, UK.
Daniel J RigdenUniversity of Liverpool, Department of Biochemistry, Cell and Systems Biology, Liverpool L69 7ZB, UK.
Jason L ParsonsUniversity of Birmingham, Institute of Cancer and Genomic Sciences, IBR West, Birmingham B15 2TT, UK.
Gabrielle J GrundyUniversity of Liverpool, Department of Molecular and Clinical Cancer Medicine, 6 West Derby St, Liverpool L7 8TX, UK. Electronic address: ggrundy@liverpool.ac.uk.
University of Liverpool · GBCancer Research UK Clinical Trials Unit · GBEdge Hill University · GB

Funding

Realizing the radiobiological impact of protons and high-LET particles in head and neck cancer and glioblastoma modelsR01CA256854 · NCI · UNIVERSITY OF LIVERPOOL · PI PARSONS, JASON · 2021 to 2025
$1.7M
Medical Research Council MR/V028944/1Medical Research Council MR/V028944/2NCI NIH HHS R01 CA256854
6 · The paper itself

Abstract

Certain members of the ADP-ribosyltransferase superfamily (ARTD or PARP enzymes) catalyse ADP-ribosylation in response to cellular stress, DNA damage and viral infection and are upregulated in various tumours. PARP9, its binding partner DTX3L and PARP14 protein levels are significantly correlated in head and neck squamous cell carcinoma (HNSCC) and other tumour types though a mechanism where PARP9/DTX3L regulates PARP14 post-transcriptionally. Depleting PARP9, DTX3L or PARP14 expression in HNSCC or HeLa cell lines decreases cell survival through a reduction of proliferation and an increase in apoptosis. A partial rescue of survival was achieved by expressing a PARP14 truncation containing a predicted eukaryotic type I KH domain. KH-like domains were also found in PARP9 and in DTX3L and contributed to protein-protein interactions between PARP9-DTX3L and PARP14-DTX3L. Homodimerization of DTX3L was also coordinated by a KH-like domain and was disrupted by site-specific mutation. Although, cell survival promoted by PARP14 did not require ADP-ribosyltransferase activity, interaction of DTX3L in vitro suppressed PARP14 auto-ADP-ribosylation and promoted trans-ADP-ribosylation of PARP9 and DTX3L. In summary, we characterised PARP9-DTX3L-PARP14 interactions important to pro-survival signalling in HNSCC cells, albeit in PARP14 catalytically independent fashion.

Indexed as

Head and Neck NeoplasmsNeoplasm ProteinsPoly(ADP-ribose) PolymerasesSquamous Cell Carcinoma of Head and NeckUbiquitin-Protein LigasesCell SurvivalHeLa CellsHumansProtein DomainsDTX3L protein, humanNeoplasm ProteinsPARP14 protein, humanPARP9 protein, humanPoly(ADP-ribose) PolymerasesUbiquitin-Protein LigasesADP-ribosylationalphafold2macro-PARPprotein–protein interactionregulation of expression

Identifiers

PMID38182103
PMCPMC11080071
OpenAlexW4390562733

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.