Evidence map›Paper›PMID 28077578›Full record

ArticleThe Journal of biological chemistry2017

Novel Serine 176 Phosphorylation of YBX1 Activates NF-κB in Colon Cancer.

Matthew Martin, Laiqing Hua, Benlian Wang, Han Wei, Lakshmi Prabhu, Antja-Voy Hartley, Guanglong Jiang, Yunlong Liu, Tao Lu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

47 citing papers in PubMed, 61 citations in OpenAlex.

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  13. YB-1 activating cascades as potential targets in KRAS-mutated tumors.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2023
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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

9 authors at 2 institutions in 1 country.

Matthew MartinDepartments of Pharmacology and Toxicology.
Laiqing HuaDepartments of Pharmacology and Toxicology.
Benlian WangCenter for Proteomics and Bioinformatics, Case Western Reserve University, Cleveland, Ohio 44106.
Han WeiDepartments of Pharmacology and Toxicology.
Lakshmi PrabhuDepartments of Pharmacology and Toxicology.
Antja-Voy HartleyDepartments of Pharmacology and Toxicology.
Guanglong JiangMedical and Molecular Genetics, Indiana University School of Medicine, Indianapolis, Indiana 46202.
Yunlong LiuMedical and Molecular Genetics, Indiana University School of Medicine, Indianapolis, Indiana 46202.
Tao LuDepartments of Pharmacology and Toxicology; Medical and Molecular Genetics, Indiana University School of Medicine, Indianapolis, Indiana 46202; Biochemistry and Molecular Biology. Electronic address: lut@iupui.edu.
Indiana University School of MedicineCase Western Reserve University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Y box protein 1 (YBX1) is a well known oncoprotein that has tumor-promoting functions. YBX1 is widely considered to be an attractive therapeutic target in cancer. To develop novel therapeutics to target YBX1, it is of great importance to understand how YBX1 is finely regulated in cancer. Previously, we have shown that YBX1 could function as a tumor promoter through phosphorylation of its Ser-165 residue, leading to the activation of the NF-κB signaling pathway (1). In this study, using mass spectrometry analysis, we discovered a distinct phosphorylation site, Ser-176, on YBX1. Overexpression of the YBX1-S176A (serine-to-alanine) mutant in either HEK293 cells or colon cancer HT29 cells showed dramatically reduced NF-κB-activating ability compared with that of WT-YBX1, confirming that Ser-176 phosphorylation is critical for the activation of NF-κB by YBX1. Importantly, the mutant of Ser-176 and the previously reported Ser-165 sites regulate distinct groups of NF-κB target genes, suggesting the unique and irreplaceable function of each of these two phosphorylated serine residues. Our important findings could provide a novel cancer therapy strategy by blocking either Ser-176 or Ser-165 phosphorylation or both of YBX1 in colon cancer.

Indexed as

Amino Acid SequenceCell ProliferationColonColonic NeoplasmsCytokinesGene Expression Regulation, NeoplasticHEK293 CellsHT29 CellsHumansNF-kappa BPhosphorylationSerineY-Box-Binding Protein 1CytokinesNF-kappa BSerineY-Box-Binding Protein 1YBX1 protein, humancolon cancerNF-κBphosphorylationposttranslational modification (PTM)serineYBX1

Identifiers

PMID28077578
PMCPMC5336175
OpenAlexW2573608880

What Socratic 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 Socratic graph.