Evidence map›Paper›PMID 28841214›Full record

ArticleCell death and differentiation2017

Tudor-domain protein PHF20L1 reads lysine methylated retinoblastoma tumour suppressor protein.

Simon M Carr, Shonagh Munro, Cari A Sagum, Oleg Fedorov, Mark T Bedford, Nicholas B La Thangue

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell death and differentiation, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

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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

6 authors at 3 institutions in 2 countries.

Simon M CarrDepartment of Oncology, University of Oxford, Old Road Campus Research Building, Old Road Campus, Roosevelt Drive, Headington, Oxford OX3 7DQ, UK.
Shonagh MunroDepartment of Oncology, University of Oxford, Old Road Campus Research Building, Old Road Campus, Roosevelt Drive, Headington, Oxford OX3 7DQ, UK.
Cari A SagumDepartment of Molecular Carcinogenesis, The University of Texas, MD Anderson Cancer Center, Smithville, TX 77030, USA.
Oleg FedorovNuffield Department of Clinical Medicine, Structural Genomics Consortium Oxford, University of Oxford, Old Road Campus Research Building, Old Road Campus, Roosevelt Drive, Headington, Oxford OX3 7DQ, UK.
Mark T BedfordDepartment of Molecular Carcinogenesis, The University of Texas, MD Anderson Cancer Center, Smithville, TX 77030, USA.
Nicholas B La ThangueDepartment of Oncology, University of Oxford, Old Road Campus Research Building, Old Road Campus, Roosevelt Drive, Headington, Oxford OX3 7DQ, UK.
University of Oxford · GBThe University of Texas MD Anderson Cancer Center · USGenomics (United Kingdom) · GB

Funding

The Functional Analysis of the Coactivator CARM1R01DK062248 · NIDDK · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BEDFORD, MARK T. · 2002 to 2015
$4.2M
The Functional Analysis of the Coactivator CARM1R56DK062248 · NIDDK · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BEDFORD, MARK T · 2007 to 2007
$77k
Cancer Research UK 13058Cancer Research UK 20776Cancer Research UK 300/A13058Cancer Research UK A13058Medical Research Council G0500905Medical Research Council G1000807Medical Research Council G9400953NIDDK NIH HHS R01 DK062248NIDDK NIH HHS R56 DK062248Wellcome Trust 092809Wellcome Trust 092809/Z/10/Z
6 · The paper itself

Abstract

The retinoblastoma tumour suppressor protein (pRb) classically functions to regulate early cell cycle progression where it acts to enforce a number of checkpoints in response to cellular stress and DNA damage. Methylation at lysine (K) 810, which occurs within a critical CDK phosphorylation site and antagonises a CDK-dependent phosphorylation event at the neighbouring S807 residue, acts to hold pRb in the hypo-phosphorylated growth-suppressing state. This is mediated in part by the recruitment of the reader protein 53BP1 to di-methylated K810, which allows pRb activity to be effectively integrated with the DNA damage response. Here, we report the surprising observation that an additional methylation-dependent interaction occurs at K810, but rather than the di-methyl mark, it is selective for the mono-methyl K810 mark. Binding of the mono-methyl PHF20L1 reader to methylated pRb occurs on E2F target genes, where it acts to mediate an additional level of control by recruiting the MOF acetyltransferase complex to E2F target genes. Significantly, we find that the interplay between PHF20L1 and mono-methyl pRb is important for maintaining the integrity of a pRb-dependent G1-S-phase checkpoint. Our results highlight the distinct roles that methyl-lysine readers have in regulating the biological activity of pRb.

Indexed as

Cell CycleCell Line, TumorChromosomal Proteins, Non-HistoneGenes, Tumor SuppressorHistone AcetyltransferasesHumansLysineMCF-7 CellsMethylationRetinoblastoma ProteinTransfectionTumor Suppressor p53-Binding Protein 1Chromosomal Proteins, Non-HistoneHistone AcetyltransferasesLysinePHF20L1 protein, humanRetinoblastoma ProteinTP53BP1 protein, humanTumor Suppressor p53-Binding Protein 1

Identifiers

PMID28841214
PMCPMC5686351
OpenAlexW2749157570

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.