Evidence map›Paper›PMID 23319590›Full record

ArticleThe Journal of biological chemistry2013

SCF(Fbxw15) mediates histone acetyltransferase binding to origin recognition complex (HBO1) ubiquitin-proteasomal degradation to regulate cell proliferation.

Chunbin Zou, Yan Chen, Rebecca M Smith, Courtney Snavely, Jin Li, Tiffany A Coon, Bill B Chen, Yutong Zhao, Rama K Mallampalli

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

33 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Role of LMO7 in cancer (Review).Oncology reports · 2024
    Review
  9. Acetyltransferase in cardiovascular disease and aging.The journal of cardiovascular aging · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. The Protective Effect of HBO1 on Cigarette Smoke Extract-Induced Apoptosis in Airway Epithelial Cells.International journal of chronic obstructive pulmonary disease · 2020
    Article
  17. Article
  18. LPS promotes HBO1 stability via USP25 to modulate inflammatory gene transcription in THP-1 cells.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018
    Article
  19. Review
  20. Review
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

9 authors at 2 institutions in 2 countries.

Chunbin ZouDepartment of Medicine, Acute Lung Injury Center of Excellence, University of Pittsburgh, Pittsburgh, Pennsylvania 15213, USA.
Yan Chen
Rebecca M Smith
Courtney Snavely
Jin Li
Tiffany A Coon
Bill B Chen
Yutong Zhao
Rama K Mallampalli
University of Pittsburgh · USSecond Xiangya Hospital of Central South University · CN

Funding

F box-Induced Acute Lung Injury and ParkinR01HL096376 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MALLAMPALLI, RAMA K · 2010 to 2025
$5.1M
Sepsis-Associated Immune Suppression and F-box ProteinsR01HL097376 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MALLAMPALLI, RAMA K · 2009 to 2025
$5.1M
Stabilizing mitochondria in sepsisR01HL098174 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI MALLAMPALLI, RAMA K · 2010 to 2021
$3.6M
Regulation of Innate Immunity by F-Box ProteinsR01HL116472 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CHEN, BEIBEI · 2013 to 2017
$1.9M
Regulation of the IL-33 receptor, ST2L, by Protein Stability in Septic InjuryR01HL112791 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ZHAO, YUTONG · 2013 to 2016
$1.5M
SCF-based Ubiquitin E3 Ligases in the Pathobiology of PneumoniaI01BX002200 · VA · VETERANS HEALTH ADMINISTRATION · PI MALLAMPALLI, RAMA K · 2014 to 2017
–
BLRD VA I01 BX002200NHLBI NIH HHS HL01916NHLBI NIH HHS HL096376NHLBI NIH HHS HL097376NHLBI NIH HHS HL098174NHLBI NIH HHS HL116472NHLBI NIH HHS R01 HL096376NHLBI NIH HHS R01 HL097376NHLBI NIH HHS R01 HL098174NHLBI NIH HHS R01 HL112791NHLBI NIH HHS R01 HL116472
6 · The paper itself

Abstract

Histone acetyltransferase binding to origin recognition complex (HBO1) plays a crucial role in DNA replication licensing and cell proliferation, yet its molecular regulation in cells is relatively unknown. Here an uncharacterized protein, Fbxw15, directly interacts with HBO1, a labile protein (t½ = ∼3 h), to mediate its ubiquitination (Lys(338)) and degradation in the cytoplasm. Fbxw15-mediated HBO1 depletion required mitogen-activated protein kinase 1 (Mek1), which was sufficient to trigger HBO1 phosphorylation and degradation in cells. Mek1 ability to produce HBO1 degradation was blocked by Fbxw15 silencing. Lipopolysaccharide induced HBO1 degradation, an effect abrogated by Fbxw15 or Mek1 cellular depletion. Modulation of Fbxw15 levels was able to differentially regulate histone H3K14 acetylation and cellular proliferation by altering HBO1 levels. These studies authenticate Fbxw15 as a ubiquitin E3 ligase subunit that mediates endotoxin-induced HBO1 depletion in cells, thereby controlling cell replicative capacity.

Indexed as

Cell ProliferationProteolysisAcetylationAnimalsCell LineF-Box ProteinsGene SilencingHistone AcetyltransferasesHistonesHumansMAP Kinase Kinase 1MiceProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein LigasesF-Box ProteinsFbxw15 protein, mouseHistone AcetyltransferasesHistonesKAT7 protein, humanKat7 protein, mouseMAP2K1 protein, humanMap2k1 protein, mouseMAP Kinase Kinase 1Proteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID23319590
PMCPMC3585065
OpenAlexW1964505185

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.