Evidence map›Paper›PMID 24811176›Full record

ArticleThe Journal of biological chemistry2014

A splicing variant of NME1 negatively regulates NF-κB signaling and inhibits cancer metastasis by interacting with IKKβ.

Dong-Joo You, Cho Rong Park, Hyun Bok Lee, Mi Jin Moon, Ju-Hee Kang, Cheolju Lee, Seong-Hyun Oh, Curie Ahn, Jae Young Seong, Jong-Ik Hwang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 25 citations in OpenAlex.

  1. Review
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  7. The actions of NME1/NDPK-A and NME2/NDPK-B as protein kinases.Laboratory investigation; a journal of technical methods and pathology · 2018
    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

10 authors at 5 institutions in 1 country.

Dong-Joo YouFrom the Graduate School of Medicine, Korea University, 73 Inchon-ro, Seongbuk-gu, Seoul 136-705, Korea.
Cho Rong ParkFrom the Graduate School of Medicine, Korea University, 73 Inchon-ro, Seongbuk-gu, Seoul 136-705, Korea.
Hyun Bok LeeFrom the Graduate School of Medicine, Korea University, 73 Inchon-ro, Seongbuk-gu, Seoul 136-705, Korea.
Mi Jin MoonFrom the Graduate School of Medicine, Korea University, 73 Inchon-ro, Seongbuk-gu, Seoul 136-705, Korea.
Ju-Hee Kangthe National Cancer Center, Goyang-si, Gyeonggi-do 410-769, Korea.
Cheolju Leethe Life Sciences Division, Korea Institute of Science and Technology, Seongbuk-gu, Seoul 136-791, Korea.
Seong-Hyun Ohthe College of Pharmacy, Gachon University, Incheon 406-840, Korea, and.
Curie Ahnthe Transplantation Research Institute, Cancer Research Institute, Seoul National University, Yongun-dong, Jongno-gu, Seoul 110-799, Korea.
Jae Young SeongFrom the Graduate School of Medicine, Korea University, 73 Inchon-ro, Seongbuk-gu, Seoul 136-705, Korea.
Jong-Ik HwangFrom the Graduate School of Medicine, Korea University, 73 Inchon-ro, Seongbuk-gu, Seoul 136-705, Korea, hjibio@korea.ac.kr.
Korea University · KRGachon University · KRKorea Institute of Science and Technology · KRNational Cancer Center · KRSeoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

IKKβ functions as a principal upstream activator of the canonical NF-κB pathway by phosphorylating IκB, leading to its proteasomal degradation. Because IKKβ is considered a therapeutic target, understanding its regulation may facilitate the design of efficient regulators of this molecule. Here, we report a novel IKKβ-interacting molecule, NME1L, a splicing variant of the NME1 protein. NME1 has attracted attention in cancer research because of its antimetastatic activity and reduced expression in multiple aggressive types of cancer. However, the effect was just moderate but not dramatic in anti-cancer activities. We found that only NME1L interacts with IKKβ. Exogenous expression of NME1L resulted in a potent decrease in TNFα-stimulated NF-κB activation, whereas knockdown of NME1/NME1L with shRNA enhanced activity of NF-κB. NME1L down-regulates IKKβ signaling by blocking IKKβ-mediated IκB degradation. When NME1L was introduced into highly metastatic HT1080 cells, the mobility was efficiently inhibited. Furthermore, in a metastasis assay, NME1L-expressing cells did not colonize the lung. Based on these results, NME1L is a potent antimetastatic protein and may be a useful weapon in the fight against cancers.

Indexed as

Alternative SplicingCell Line, TumorHEK293 CellsHumansI-kappa B KinaseNeoplasm MetastasisNeoplasm ProteinsNeoplasmsNF-kappa BNM23 Nucleoside Diphosphate KinasesI-kappa B KinaseNeoplasm ProteinsNF-kappa BNM23 Nucleoside Diphosphate KinasesNME1 protein, humanCancerIKKbetaInvasionMetastasisMigrationNF-kappaBNME1L

Identifiers

PMID24811176
PMCPMC4067205
OpenAlexW2163248716

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.