Evidence map›Paper›PMID 29093443›Full record

ArticleNature communications2017

Endosomal phosphatidylserine is critical for the YAP signalling pathway in proliferating cells.

Tatsuyuki Matsudaira, Kojiro Mukai, Taishin Noguchi, Junya Hasegawa, Tomohisa Hatta, Shun-Ichiro Iemura, Tohru Natsume, Norio Miyamura, Hiroshi Nishina, Jun Nakayama and 5 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

32 citing papers in PubMed, 59 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

15 authors at 6 institutions in 1 country.

Tatsuyuki MatsudairaDepartment of Health Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Kojiro MukaiDepartment of Health Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Taishin NoguchiDepartment of Health Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Junya HasegawaDepartment of Health Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Tomohisa HattaMolecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology, 2-3-26, Aomi, Koto-ku, Tokyo, 135-0064, Japan.
Shun-Ichiro IemuraMedical Industry Translational Research Center, Fukushima Medical University, 1, Hikarigaoka, Fukushima, 960-1295, Japan.
Tohru NatsumeMolecular Profiling Research Center for Drug Discovery, National Institute of Advanced Industrial Science and Technology, 2-3-26, Aomi, Koto-ku, Tokyo, 135-0064, Japan.
Norio MiyamuraDepartment of Developmental and Regenerative Biology, Medical Research Institute, Tokyo Medical and Dental University, 1-5-45, Yushima, Bunkyo-ku, Tokyo, 113-8519, Japan.
Hiroshi NishinaDepartment of Developmental and Regenerative Biology, Medical Research Institute, Tokyo Medical and Dental University, 1-5-45, Yushima, Bunkyo-ku, Tokyo, 113-8519, Japan.
Jun NakayamaDepartment of Life Science and Medical Bioscience, School of Advanced Science and Engineering, Waseda University, 2-2, Wakamatsu-cho, Shinjuku-ku, Tokyo, 162-8480, Japan.
Kentaro SembaDepartment of Life Science and Medical Bioscience, School of Advanced Science and Engineering, Waseda University, 2-2, Wakamatsu-cho, Shinjuku-ku, Tokyo, 162-8480, Japan.
Takuya TomitaLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.
Shigeo MurataLaboratory of Protein Metabolism, Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.ORCID http://orcid.org/0000-0002-3177-3503
Hiroyuki AraiDepartment of Health Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan. harai@mol.f.u-tokyo.ac.jp.
Tomohiko TaguchiDepartment of Health Chemistry, Graduate School of Pharmaceutical Sciences, University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan. tom_taguchi@mol.f.u-tokyo.ac.jp.ORCID http://orcid.org/0000-0003-0464-6370
The University of Tokyo · JPNational Institute of Advanced Industrial Science and Technology · JPTokyo Medical and Dental University · JPWaseda University · JPFukushima Medical University · JPJapan Agency for Medical Research and Development · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Yes-associated protein (YAP) is a recently discovered growth-promoting transcription coactivator that has been shown to regulate the malignancy of various cancers. How YAP is regulated is not fully understood. Here, we show that one of the factors regulating YAP is phosphatidylserine (PS) in recycling endosomes (REs). We use proximity biotinylation to find proteins proximal to PS. Among these proteins are YAP and multiple proteins related to YAP signalling. Knockdown of ATP8A1 (an RE PS-flippase) or evectin-2 (an RE-resident protein) and masking of PS in the cytoplasmic leaflet of membranes, all suppress nuclear localization of YAP and YAP-dependent transcription. ATP8A1 knockdown increases the phosphorylated (activated) form of Lats1 that phosphorylates and inactivates YAP, whereas evectin-2 knockdown reduces the ubiquitination and increased the level of Lats1. The proliferation of YAP-dependent metastatic cancer cells is suppressed by knockdown of ATP8A1 or evectin-2. These results suggest a link between a membrane phospholipid and cell proliferation.

Indexed as

Adaptor Proteins, Signal TransducingAdenosine TriphosphatasesAnimalsBiotinylationCell NucleusCell ProliferationChlorocebus aethiopsCOS CellsEndosomesGene Knockdown TechniquesHEK293 CellsHumansMembrane ProteinsPhosphatidylserinesPhospholipid Transfer ProteinsPhosphoproteinsAdaptor Proteins, Signal TransducingAdenosine TriphosphatasesATP8A1 protein, humanLATS1 protein, humanMembrane ProteinsPhosphatidylserinesPhospholipid Transfer ProteinsPhosphoproteinsPLEKHB2 protein, humanProtein Serine-Threonine KinasesTranscription FactorsYAP1 protein, humanYAP-Signaling Proteins

Identifiers

PMID29093443
PMCPMC5665887
OpenAlexW2766714008

What OpenQuestion holds

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LicenceCC BY
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.