Evidence map›Paper›PMID 24637302›Full record

ArticleCellular signalling2014

PMA induces SnoN proteolysis and CD61 expression through an autocrine mechanism.

Chonghua Li, Natoya Peart, Zhenyu Xuan, Dorothy E Lewis, Yang Xia, Jianping Jin

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

Article in Cellular signalling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. The Involvement of Canonical NFκB Pathway in Megakaryocyte Differentiation Induction by Nanocurcumin.International journal of hematology-oncology and stem cell research · 2023
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  2. Review
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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 2 institutions in 1 country.

Chonghua LiDepartment of Biochemistry and Molecular Biology, Medical School, United States.
Natoya PeartDepartment of Biochemistry and Molecular Biology, Medical School, United States; Program of Biochemistry and Molecular Biology, Graduate School of Biomedical Sciences, The University of Texas Health Science Center at Houston, Houston, TX 77030, United States.
Zhenyu XuanDepartment of Molecular and Cellular Biology, The University of Texas at Dallas, Dallas, TX, United States.
Dorothy E LewisDepartment of Internal Medicine, Medical School, United States.
Yang XiaDepartment of Biochemistry and Molecular Biology, Medical School, United States; Program of Biochemistry and Molecular Biology, Graduate School of Biomedical Sciences, The University of Texas Health Science Center at Houston, Houston, TX 77030, United States.
Jianping JinDepartment of Biochemistry and Molecular Biology, Medical School, United States; Program of Biochemistry and Molecular Biology, Graduate School of Biomedical Sciences, The University of Texas Health Science Center at Houston, Houston, TX 77030, United States. Electronic address: Jianping.jin@uth.tmc.edu.
The University of Texas Health Science Center at Houston · USThe University of Texas at Dallas · US

Funding

Post-ubiquitinational Regulation of I-kappa-B-alpha Proteolysis under StimuliR01GM102529 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI JIN, JIANPING · 2012 to 2016
$1.4M
NIGMS NIH HHS R01 GM102529
6 · The paper itself

Abstract

Phorbol-12-myristate-13-acetate, also called PMA, is a small molecule that activates protein kinase C and functions to differentiate hematologic lineage cells. However, the mechanism of PMA-induced cellular differentiation is not fully understood. We found that PMA triggers global enhancement of protein ubiquitination in K562, a myelogenous leukemia cell line and one of the enhanced-ubiquitination targets is SnoN, an inhibitor of the Smad signaling pathway. Our data indicated that PMA stimulated the production of Activin A, a cytokine of the TGF-β family. Activin A then activated the phosphorylation of both Smad2 and Smad3. In consequence, SnoN is ubiquitinated by the APC(Cdh1) ubiquitin ligase with the help of phosphorylated Smad2. Furthermore, we found that SnoN proteolysis is important for the expression of CD61, a marker of megakaryocyte. These results indicate that protein ubiquitination promotes megakaryopoiesis via degrading SnoN, an inhibitor of CD61 expression, strengths the roles of ubiquitination in cellular differentiation.

Indexed as

Activin Receptors, Type IActivin Receptors, Type IIActivinsAntigens, CDCadherinsCarcinogensCell Line, TumorHumansIntegrin beta3Intracellular Signaling Peptides and ProteinsPhosphorylationProtein Kinase CProteolysisProto-Oncogene ProteinsRNA InterferenceRNA, Small Interferingactivin AActivin Receptors, Type IActivin Receptors, Type IIactivin receptor type II-AActivinsACVR1B protein, humanAntigens, CDCadherinsCarcinogensCDH1 protein, humanIntegrin beta3Intracellular Signaling Peptides and ProteinsITGB3 protein, humanProtein Kinase CProto-Oncogene ProteinsRNA, Small InterferingSKIL protein, humanSmad2 ProteinSMAD2 protein, humanSmad3 ProteinSMAD3 protein, humanTetradecanoylphorbol AcetateUbiquitinUbiquitin-Protein LigasesActivin ACdh1DifferentiationSmad2SnoNUbiquitin

Identifiers

PMID24637302
PMCPMC4074601
OpenAlexW2047718234

What OpenQuestion holds

Textmetadata
LicenceTDM
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.