Evidence map›Paper›PMID 26862730›Full record

ArticleOncotarget2016

Ras-activated RSK1 phosphorylates EBP50 to regulate its nuclear localization and promote cell proliferation.

Hooi Cheng Lim, Tzuu-Shuh Jou

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Hooi Cheng LimGraduate Institute of Molecular Medicine, National Taiwan University, Taipei, Taiwan.
Tzuu-Shuh JouGraduate Institute of Molecular Medicine, National Taiwan University, Taipei, Taiwan.
National Taiwan University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Differential subcellular localization of EBP50 leads to its controversial role in cancer biology either as a tumor suppressor when it resides at the membrane periphery, or a tumor facilitator at the nucleus. However, the mechanism behind nuclear localization of EBP50 remains unclear. A RNA interference screening identified the downstream effector of the Ras-ERK cascade, RSK1, as the molecule unique for nuclear transport of EBP50. RSK1 binds to EBP50 and phosphorylates it at a conserved threonine residue at position 156 (T156) under the regulation of growth factor. Mutagenesis experiments confirmed the significance of T156 residue in nuclear localization of EBP50, cellular proliferation, and oncogenic transformation. Our study sheds light on a possible therapeutic strategy targeting at this aberrant nuclear expression of EBP50 without affecting the normal physiological function of EBP50 at other subcellular localization.

Indexed as

Active Transport, Cell NucleusAnimalsBinding SitesCell Line, TumorCell NucleusCell ProliferationHEK293 CellsHeLa CellsHumansMiceMice, Inbred NODMice, SCIDPhosphoproteinsPhosphorylationProtein BindingRibosomal Protein S6 Kinases, 90-kDaPhosphoproteinsRibosomal Protein S6 Kinases, 90-kDaRNA, Small InterferingRPS6KA1 protein, humansodium-hydrogen exchanger regulatory factorSodium-Hydrogen ExchangersEBP50nuclear localizationphosphorylationproliferationRSK1

Identifiers

PMID26862730
PMCPMC4891120
OpenAlexW2291627101

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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.