Evidence map›Paper›PMID 31089935›Full record

ArticleMolecular and cellular biochemistry2019

DBS is activated by EPHB2/SRC signaling-mediated tyrosine phosphorylation in HEK293 cells.

Shun Nakano, Masashi Nishikawa, Rina Asaoka, Natsuko Ishikawa, Chisato Ohwaki, Katsuya Sato, Hitoshi Nagaoka, Hisashi Yamakawa, Takahiro Nagase, Hiroshi Ueda

Abstract read
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In one paragraph

Article in Molecular and cellular biochemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 44% 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

4 citing papers in PubMed, 4 citations in OpenAlex.

  1. 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 2 institutions in 1 country.

Shun NakanoUnited Graduate School of Drug Discovery and Medical Information Sciences, Gifu University, Yanagido1-1, Gifu, 501-1193, Japan.
Masashi NishikawaUnited Graduate School of Drug Discovery and Medical Information Sciences, Gifu University, Yanagido1-1, Gifu, 501-1193, Japan.
Rina AsaokaBiomolecular Science Division, Faculty of Engineering, Gifu University, Yanagido1-1, Gifu, 501-1193, Japan.
Natsuko IshikawaDepartment of Life Science and Chemistry, Graduate School of Natural Science and Technology, Gifu University, 1-1 Yanagido, Gifu, 501-1193, Japan.
Chisato OhwakiDepartment of Life Science and Chemistry, Graduate School of Natural Science and Technology, Gifu University, 1-1 Yanagido, Gifu, 501-1193, Japan.
Katsuya SatoDepartment of Molecular Pathobiochemistry, Gifu University Graduate School of Medicine, Yanagido 1-1, Gifu, 501-1193, Japan.
Hitoshi NagaokaDepartment of Molecular Pathobiochemistry, Gifu University Graduate School of Medicine, Yanagido 1-1, Gifu, 501-1193, Japan.
Hisashi YamakawaKazusa DNA Research Institute, Chiba, 293-0818, Japan.
Takahiro NagaseKazusa DNA Research Institute, Chiba, 293-0818, Japan.
Hiroshi UedaUnited Graduate School of Drug Discovery and Medical Information Sciences, Gifu University, Yanagido1-1, Gifu, 501-1193, Japan. hueda@gifu-u.ac.jp.ORCID http://orcid.org/0000-0003-3311-877X
Gifu University · JPKazusa DNA Research Institute · JP

Funding

Japan Society for the Promotion of Science KAKENHI Grant Number 15K07927Japan Society for the Promotion of Science KAKENHI Grant Number 23590073
6 · The paper itself

Abstract

It is well known that Rho family small GTPases (Rho GTPase) has a role of molecular switch in intracellular signal transduction. The switch cycle between GTP-bound and GDP-bound state of Rho GTPase regulates various cell responses such as gene transcription, cytoskeletal rearrangements, and vesicular trafficking. Rho GTPase-specific guanine nucleotide exchange factors (RhoGEFs) are regulated by various extracellular stimuli and activates Rho GTPase such as RhoA, Rac1, and Cdc42. The molecular mechanisms that regulate RhoGEFs are poorly understood. Our studies reveal that Dbl's big sister (DBS), a RhoGEF for Cdc42 and RhoA, is phosphorylated at least on tyrosine residues at 479, 660, 727, and 926 upon stimulation by SRC signaling and that the phosphorylation at Tyr-660 is particularly critical for the serum response factor (SRF)-dependent transcriptional activation of DBS by Ephrin type-B receptor 2 (EPHB2)/SRC signaling. In addition, our studies also reveal that the phosphorylation of Tyr-479 and Tyr-660 on DBS leads to the actin cytoskeletal reorganization by EPHB2/SRC signaling. These findings are thought to be useful for understanding pathological conditions related to DBS such as cancer and non-syndromic autism in future.

Indexed as

Signal Transductioncdc42 GTP-Binding ProteinHEK293 CellsHumansReceptor, EphB2rhoA GTP-Binding ProteinRho Guanine Nucleotide Exchange Factorssrc-Family Kinasescdc42 GTP-Binding ProteinCDC42 protein, humanEPHB2 protein, humanReceptor, EphB2rhoA GTP-Binding ProteinRHOA protein, humanRho Guanine Nucleotide Exchange Factorssrc-Family KinasesEPHB2Gene transcriptionRhoGEFSRCTyrosine phosphorylation

Identifiers

PMID31089935
OpenAlexW2945605761

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.