Evidence map›Paper›PMID 29522376›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2018

Histone acetyltransferase CBP promotes function of SCF FBXL19 ubiquitin E3 ligase by acetylation and stabilization of its F-box protein subunit.

Jianxin Wei, Su Dong, Kangning Yao, Maria Francesca Ysabelle M Martinez, Paine R Fleisher, Yutong Zhao, Haichun Ma, Jing Zhao

Open access · bronzeAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. ISGylation of NF-κBp65 by SCFArteriosclerosis, thrombosis, and vascular biology · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. CREB1ACS omega · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Two distinct E3 ligases, SCFFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
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

8 authors at 2 institutions in 2 countries.

Jianxin WeiDepartment of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
Su DongDepartment of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
Kangning YaoDepartment of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
Maria Francesca Ysabelle M MartinezDepartment of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
Paine R FleisherDepartment of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
Yutong ZhaoDepartment of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
Haichun MaDepartment of Anesthesia, First Hospital of Jilin University, Changchun, China.
Jing ZhaoDepartment of Medicine, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA.
University of Pittsburgh · USJilin University · CN

Funding

Molecular regulation of anti-inflammatory cytokine receptor in sepsisR01HL136294 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ZHAO, YUTONG · 2018 to 2021
$1.8M
Regulation of proteolysis by deubiquiting enzyme in lung inflammatory diseaseR01HL131665 · NHLBI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ZHAO, YUTONG · 2017 to 2020
$1.5M
Regulation of Histone Acetyltransferase Stability In SepsisR01GM115389 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ZHAO, JING · 2015 to 2019
$1.5M
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
NHLBI NIH HHS R01 HL112791NHLBI NIH HHS R01 HL131665NHLBI NIH HHS R01 HL136294NIGMS NIH HHS R01 GM115389
6 · The paper itself

Abstract

Ubiquitin E3 ligases mediate ubiquitination and degradation of intracellular proteins. We have shown that a relatively new Skp, Cullin, F-box (SCF) protein E3 ligase, SCF FBXL19, has an anti-inflammatory effect and controls actin cytoskeleton dynamics via targeting cell membrane receptor and small GTPases for their ubiquitination and degradation, but the molecular regulation of its subunit FBXL19 stability remains unclear. Here we show that FBXL19 degradation is controlled by the balance between its ubiquitination and acetylation. FBXL19 is an unstable protein with a half-life of ∼3 h. FBXL19 can be polyubiquitinated, and the proteasome inhibitor MG-132 prolongs FBXL19 half-life, suggesting that FBXL19 degradation is mediated in the ubiquitin-proteasome system. FBXL19 can also be acetylated, and enhancing acetylation of FBXL19 by a deacetylase inhibitor reduces FBXL19 ubiquitination levels. Acetylation-mimic FBXL19 mutant exhibits a longer half-life than wild type. An acetyltransferase CBP catalyzes acetylation of FBXL19. Inhibition or down-regulation of CBP reduces FBXL19 stability, whereas it is increased in CBP-overexpressing cells. Taken together, the data indicate that CBP-mediated acetylation reduces ubiquitination and stabilizes FBXL19. Further, we demonstrate that FBXL19 targets small GTPase Cdc42 for its ubiquitination and degradation, whereas this effect is reversed by inhibition of CBP, suggesting that CBP increases the effect of SCF FBXL19 E3 ligase through acetylation and stabilization of FBXL19. Our study reveals a new molecular model for regulation of SCF E3 ligase function by acetylation and stabilization of its subunit F-box protein.-Wei, J., Dong, S., Yao, K., Martinez, M. F. Y. M., Fleisher, P. R., Zhao, Y., Ma, H., Zhao, J. Histone acetyltransferase CBP promotes function of SCF FBXL19 ubiquitin E3 ligase by acetylation and stabilization of its F-box protein subunit.

Indexed as

AcetylationAnimalsCell LineDNA-Binding ProteinsDown-RegulationHalf-LifeHistone AcetyltransferasesHumansMiceProtein SubunitsProteolysisSKP Cullin F-Box Protein LigasesUbiquitinationUbiquitin-Protein LigasesDNA-Binding ProteinsHistone AcetyltransferasesProtein SubunitsSKP Cullin F-Box Protein LigasesUbiquitin-Protein LigasesCdc42 GTPaseprotein stabilityubiquitination

Identifiers

PMID29522376
PMCPMC6191137
OpenAlexW2790688203

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.