Evidence map›Paper›PMID 33010150›Full record

ArticleNucleic acids research2020

CK2 kinase-mediated PHF8 phosphorylation controls TopBP1 stability to regulate DNA replication.

Haihua Feng, Jingchen Lu, Xiaotian Song, Angkana Thongkum, Fan Zhang, Lihong Lou, Ofer Reizes, Alexandru Almasan, Zihua Gong

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

10 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. JmjC Family of Histone Demethylases Form Nuclear Condensates.International journal of molecular sciences · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Haihua FengDepartment of Cancer Biology, Cleveland Clinic Lerner Research Institute, Cleveland, OH 44195, USA.
Jingchen LuDepartment of Cancer Biology, Cleveland Clinic Lerner Research Institute, Cleveland, OH 44195, USA.
Xiaotian SongDepartment of Cancer Biology, Cleveland Clinic Lerner Research Institute, Cleveland, OH 44195, USA.
Angkana ThongkumDepartment of Cancer Biology, Cleveland Clinic Lerner Research Institute, Cleveland, OH 44195, USA.
Fan ZhangDepartment of Cancer Biology, Cleveland Clinic Lerner Research Institute, Cleveland, OH 44195, USA.
Lihong LouDepartment of Cancer Biology, Cleveland Clinic Lerner Research Institute, Cleveland, OH 44195, USA.
Ofer ReizesDepartment of Cardiovascular & Metabolic Sciences, Cleveland Clinic Lerner Research Institute, Cleveland, OH 44195, USA.
Alexandru AlmasanDepartment of Cancer Biology, Cleveland Clinic Lerner Research Institute, Cleveland, OH 44195, USA.
Zihua GongDepartment of Cancer Biology, Cleveland Clinic Lerner Research Institute, Cleveland, OH 44195, USA.
Cleveland Clinic Lerner College of Medicine · USCentral South University · CN

Funding

The role of NUDT16 in DNA damage response and tumorigenesisR01CA222195 · NCI · CLEVELAND CLINIC LERNER COM-CWRU · PI Zihua Gong · 2019 to 2026
$3.8M
Therapeutic resistance in leukemic cells: targeting BCL-2 family and autophagyR01CA184137 · NCI · CLEVELAND CLINIC LERNER COM-CWRU · PI ALMASAN, ALEXANDRU · 2015 to 2019
$1.8M
NCI NIH HHS R01 CA184137NCI NIH HHS R01 CA222195
6 · The paper itself

Abstract

ATR functions as a master regulator of the DNA-damage response. ATR activation requires the ATR activator, topoisomerase IIβ-binding protein 1 (TopBP1). However, the underlying mechanism of TopBP1 regulation and how its regulation affects DNA replication remain unknown. Here, we report a specific interaction between TopBP1 and the histone demethylase PHF8. The TopBP1/PHF8 interaction is mediated by the BRCT 7+8 domain of TopBP1 and phosphorylation of PHF8 at Ser854. This interaction is cell-cycle regulated and phosphorylation-dependent. PHF8 is phosphorylated by CK2, which regulates binding of PHF8 to TopBP1. Importantly, PHF8 regulates TopBP1 protein level by preventing its ubiquitination and degradation mediated by the E3 ligase UBR5. Interestingly, PHF8pS854 is likely to contribute to regulation of TopBP1 stability and DNA replication checkpoint. Further, both TopBP1 and PHF8 are required for efficient replication fork restart. Together, these data identify PHF8 as a TopBP1-binding protein and provide mechanistic insight into how PHF8 regulates TopBP1 stability to maintain DNA replication.

Indexed as

DNA ReplicationAtaxia Telangiectasia Mutated ProteinsCarrier ProteinsCasein Kinase IICell LineDNA-Binding ProteinsHistone DemethylasesHumansNuclear ProteinsPhosphorylationProtein BindingProtein DomainsTranscription FactorsAtaxia Telangiectasia Mutated ProteinsATR protein, humanCarrier ProteinsCasein Kinase IIDNA-Binding ProteinsHistone DemethylasesNuclear ProteinsPHF8 protein, humanTOPBP1 protein, humanTranscription Factors

Identifiers

PMID33010150
PMCPMC7641741
OpenAlexW3089737836

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.