Evidence map›Paper›PMID 27979972›Full record

ArticleEMBO reports2017

Phosphorylation by NLK inhibits YAP-14-3-3-interactions and induces its nuclear localization.

Sungho Moon, Wantae Kim, Soyoung Kim, Youngeun Kim, Yonghee Song, Oleksii Bilousov, Jiyoung Kim, Taebok Lee, Boksik Cha, Minseong Kim and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in EMBO reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
8.5field-weighted citation impact, top 2% 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

112 citing papers in PubMed, 175 citations in OpenAlex.

  1. Article
  2. Article
  3. The Regulation and Function of Hippo/YAP Pathway in Cancer.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Review
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52 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 3 countries.

Sungho MoonDepartment of Life Science, University of Seoul, Seoul, Korea.ORCID 0000-0002-5938-8930
Wantae KimDepartment of Life Science, University of Seoul, Seoul, Korea.
Soyoung KimDepartment of Life Science, University of Seoul, Seoul, Korea.
Youngeun KimDepartment of Life Science, University of Seoul, Seoul, Korea.
Yonghee SongDepartment of Life Science, University of Seoul, Seoul, Korea.
Oleksii BilousovDepartment of Pharmacology and Toxicology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland.
Jiyoung KimDepartment of Life Science, University of Seoul, Seoul, Korea.
Taebok LeeDepartment of Life Science, University of Seoul, Seoul, Korea.
Boksik ChaDepartment of Life Science, University of Seoul, Seoul, Korea.
Minseong KimDepartment of Life Science, University of Seoul, Seoul, Korea.
Hanjun KimDepartment of Life Science, University of Seoul, Seoul, Korea.
Vladimir L KatanaevDepartment of Pharmacology and Toxicology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland vladimir.katanaev@unil.ch ej70@uos.ac.kr.
Eek-Hoon JhoDepartment of Life Science, University of Seoul, Seoul, Korea vladimir.katanaev@unil.ch ej70@uos.ac.kr.ORCID 0000-0003-2414-6234
University of Seoul · KRFar Eastern Federal University · RUUniversity of Lausanne · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hippo signaling controls organ size by regulating cell proliferation and apoptosis. Yes-associated protein (YAP) is a key downstream effector of Hippo signaling, and LATS-mediated phosphorylation of YAP at Ser127 inhibits its nuclear localization and transcriptional activity. Here, we report that Nemo-like kinase (NLK) phosphorylates YAP at Ser128 both in vitro and in vivo, which blocks interaction with 14-3-3 and enhances its nuclear localization. Depletion of NLK increases YAP phosphorylation at Ser127 and reduces YAP-mediated reporter activity. These results suggest that YAP phosphorylation at Ser128 and at Ser127 may be mutually exclusive. We also find that with the increase in cell density, nuclear localization and the level of NLK are reduced, resulting in reduction in YAP phosphorylation at Ser128. Furthermore, knockdown of Nemo (the Drosophila NLK) in fruit fly wing imaginal discs results in reduced expression of the Yorkie (the Drosophila YAP) target genes expanded and DIAP1, while Nemo overexpression reciprocally increased the expression. Overall, our data suggest that NLK/Nemo acts as an endogenous regulator of Hippo signaling by controlling nuclear localization and activity of YAP/Yorkie.

Indexed as

14-3-3 ProteinsAmino Acid SequenceAnimalsCell CountCell Cycle ProteinsCell LineCell MovementCell NucleusDrosophilaHumansIntracellular Signaling Peptides and ProteinsMiceNuclear ProteinsPhosphorylationProtein BindingProtein Serine-Threonine Kinases14-3-3 ProteinsCell Cycle ProteinsIntracellular Signaling Peptides and ProteinsNLK protein, humanNuclear ProteinsProtein Serine-Threonine KinasesSerineTranscription FactorsYY1AP1 protein, human14‐3‐3cell densityHippo signalingNLKYAP

Identifiers

PMID27979972
PMCPMC5210122
OpenAlexW2565967823

What OpenQuestion holds

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Registered trials

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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.