Evidence map›Paper›PMID 27765816›Full record

ArticleThe Journal of biological chemistry2016

Four-and-a-half LIM Domains 1 (FHL1) Protein Interacts with the Rho Guanine Nucleotide Exchange Factor PLEKHG2/FLJ00018 and Regulates Cell Morphogenesis.

Katsuya Sato, Masashi Kimura, Kazue Sugiyama, Masashi Nishikawa, Yukio Okano, Hitoshi Nagaoka, Takahiro Nagase, Yukio Kitade, Hiroshi Ueda

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.9field-weighted citation impact, top 21% 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

8 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

9 authors at 3 institutions in 2 countries.

Katsuya SatoFrom the United Graduate School of Drug Discovery and Medical Information Sciences and.
Masashi Kimurathe Department of Molecular Pathobiochemistry, Gifu University Graduate School of Medicine, Yanagido 1-1, Gifu 501-1193, Japan.
Kazue SugiyamaFrom the United Graduate School of Drug Discovery and Medical Information Sciences and.
Masashi NishikawaFrom the United Graduate School of Drug Discovery and Medical Information Sciences and.
Yukio Okanothe Department of Molecular Pathobiochemistry, Gifu University Graduate School of Medicine, Yanagido 1-1, Gifu 501-1193, Japan.
Hitoshi Nagaokathe Department of Molecular Pathobiochemistry, Gifu University Graduate School of Medicine, Yanagido 1-1, Gifu 501-1193, Japan.
Takahiro Nagasethe Kazusa DNA Research Institute, 2-6-7 Kazusa-kamatari, Kisarazu, Chiba 292-0818, Japan, and.
Yukio KitadeFrom the United Graduate School of Drug Discovery and Medical Information Sciences and.
Hiroshi UedaFrom the United Graduate School of Drug Discovery and Medical Information Sciences and hueda@gifu-u.ac.jp.
Gifu University · JPGraduate School USA · USKazusa DNA Research Institute · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PLEKHG2/FLJ00018 is a Gβγ-dependent guanine nucleotide exchange factor for the small GTPases Rac and Cdc42 and has been shown to mediate the signaling pathways leading to actin cytoskeleton reorganization. Here we showed that the zinc finger domain-containing protein four-and-a-half LIM domains 1 (FHL1) acts as a novel interaction partner of PLEKHG2 by the yeast two-hybrid system. Among the isoforms of FHL1 (i.e. FHL1A, FHL1B, and FHL1C), FHL1A and FHL1B interacted with PLEKHG2. We found that there was an FHL1-binding region at amino acids 58-150 of PLEKHG2. The overexpression of FHL1A but not FHL1B enhanced the PLEKHG2-induced serum response element-dependent gene transcription. The co-expression of FHL1A and Gβγ synergistically enhanced the PLEKHG2-induced serum response element-dependent gene transcription. Increased transcription activity was decreased by FHL1A knock-out with the CRISPR/Cas9 system. Compared with PLEKHG2-expressing cells, the number and length of finger-like protrusions were increased in PLEKHG2-, Gβγ-, and FHL1A-expressing cells. Our results provide evidence that FHL1A interacts with PLEKHG2 and regulates cell morphological change through the activity of PLEKHG2.

Indexed as

Guanine Nucleotide Exchange FactorsHEK293 CellsHumansIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMuscle ProteinsProtein IsoformsSerum Response ElementTranscription, GeneticFHL1 protein, humanGuanine Nucleotide Exchange FactorsIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMuscle ProteinsPLEKHG2 protein, humanProtein IsoformsG proteinguanine nucleotide exchange factor (GEF)protein-protein interactionRho (Rho GTPase)yeast two-hybrid

Identifiers

PMID27765816
PMCPMC5122788
OpenAlexW2535329281

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.