Evidence map›Paper›PMID 26572825›Full record

ArticleMolecular and cellular biology2016

UV Damage-Induced Phosphorylation of HBO1 Triggers CRL4DDB2-Mediated Degradation To Regulate Cell Proliferation.

Ryoichi Matsunuma, Hiroyuki Niida, Tatsuya Ohhata, Kyoko Kitagawa, Satoshi Sakai, Chiharu Uchida, Bunsyo Shiotani, Masaki Matsumoto, Keiichi I Nakayama, Hiroyuki Ogura and 2 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2016. 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 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
1.2field-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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
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  18. Article
  19. The emerging role for Cullin 4 family of E3 ligases in tumorigenesis.Biochimica et biophysica acta. Reviews on cancer · 2019
    Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

12 authors at 3 institutions in 1 country.

Ryoichi MatsunumaDepartment of Molecular Biology, Hamamatsu University School of Medicine, Shizuoka, Japan First Department of Surgery, Hamamatsu University School of Medicine, Shizuoka, Japan.
Hiroyuki NiidaDepartment of Molecular Biology, Hamamatsu University School of Medicine, Shizuoka, Japan niidah@hama-med.ac.jp.
Tatsuya OhhataDepartment of Molecular Biology, Hamamatsu University School of Medicine, Shizuoka, Japan.
Kyoko KitagawaDepartment of Molecular Biology, Hamamatsu University School of Medicine, Shizuoka, Japan.
Satoshi SakaiDepartment of Molecular Biology, Hamamatsu University School of Medicine, Shizuoka, Japan.
Chiharu UchidaDepartment of Molecular Biology, Hamamatsu University School of Medicine, Shizuoka, Japan Research Equipment Center, Hamamatsu University School of Medicine, Shizuoka, Japan.
Bunsyo ShiotaniDepartment of Cellular and Molecular Biology, Hiroshima University, Hiroshima, Japan.
Masaki MatsumotoDepartment of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Keiichi I NakayamaDepartment of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Hiroyuki OguraFirst Department of Surgery, Hamamatsu University School of Medicine, Shizuoka, Japan.
Norihiko ShiiyaFirst Department of Surgery, Hamamatsu University School of Medicine, Shizuoka, Japan.
Masatoshi KitagawaDepartment of Molecular Biology, Hamamatsu University School of Medicine, Shizuoka, Japan.
Hamamatsu University School of Medicine · JPKyushu University · JPHiroshima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone acetyltransferase binding to ORC-1 (HBO1) is a critically important histone acetyltransferase for forming the prereplicative complex (pre-RC) at the replication origin. Pre-RC formation is completed by loading of the MCM2-7 heterohexameric complex, which functions as a helicase in DNA replication. HBO1 recruited to the replication origin by CDT1 acetylates histone H4 to relax the chromatin conformation and facilitates loading of the MCM complex onto replication origins. However, the acetylation status and mechanism of regulation of histone H3 at replication origins remain elusive. HBO1 positively regulates cell proliferation under normal cell growth conditions. Whether HBO1 regulates proliferation in response to DNA damage is poorly understood. In this study, we demonstrated that HBO1 was degraded after DNA damage to suppress cell proliferation. Ser50 and Ser53 of HBO1 were phosphorylated in an ATM/ATR DNA damage sensor-dependent manner after UV treatment. ATM/ATR-dependently phosphorylated HBO1 preferentially interacted with DDB2 and was ubiquitylated by CRL4(DDB2). Replacement of endogenous HBO1 in Ser50/53Ala mutants maintained acetylation of histone H3K14 and impaired cell cycle regulation in response to UV irradiation. Our findings demonstrate that HBO1 is one of the targets in the DNA damage checkpoint. These results show that ubiquitin-dependent control of the HBO1 protein contributes to cell survival during UV irradiation.

Indexed as

AcetylationCell ProliferationDNA-Binding ProteinsDNA DamageHEK293 CellsHeLa CellsHistone AcetyltransferasesHistonesHumansPhosphorylationPoint MutationProtein Interaction MapsProtein StabilityProteolysisReceptors, Interleukin-17UbiquitinDDB2 protein, humanDNA-Binding ProteinsHistone AcetyltransferasesHistonesIL17RB protein, humanKAT7 protein, humanReceptors, Interleukin-17UbiquitinUbiquitin-Protein Ligases

Identifiers

PMID26572825
PMCPMC4719422
OpenAlexW2200622233

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.