Evidence map›Paper›PMID 29377108›Full record

ReviewJournal of cellular physiology2018

Regulation of RhoA GTPase and various transcription factors in the RhoA pathway.

Jae-Gyu Kim, Rokibul Islam, Jung Y Cho, Hwalrim Jeong, Kim-Cuong Cap, Yohan Park, Abu J Hossain, Jae-Bong Park

Abstract readReview
In one paragraph

Review in Journal of cellular physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed, 1 pooled it
4.9field-weighted citation impact, top 4% 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

82 citing papers in PubMed, 1 synthesis or guideline pooled it, 124 citations in OpenAlex.

  1. Pooled it
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  10. Functions of RhoA in the female reproductive system.Reproductive and developmental medicine · 2025
    Review
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22 more citing papers are in PubMed but not listed here.

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

8 authors at 1 institution in 1 country.

Jae-Gyu KimDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, Republic of Korea.
Rokibul IslamDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, Republic of Korea.
Jung Y ChoDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, Republic of Korea.
Hwalrim JeongDepartment of Paediatrics, Chuncheon Sacred Hospital Hallym University, Chuncheon, Kangwon-do, Republic of Korea.
Kim-Cuong CapDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, Republic of Korea.
Yohan ParkDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, Republic of Korea.
Abu J HossainDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, Republic of Korea.
Jae-Bong ParkDepartment of Biochemistry, Hallym University College of Medicine, Chuncheon, Kangwon-do, Republic of Korea.ORCID http://orcid.org/0000-0003-2323-4742
Hallym University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RhoA GTPase plays a variety of functions in regulation of cytoskeletal proteins, cellular morphology, and migration along with various proliferation and transcriptional activity in cells. RhoA activity is regulated by guanine nucleotide exchange factors (GEFs), GTPase activating proteins (GAPs), and the guanine nucleotide dissociation factor (GDI). The RhoA-RhoGDI complex exists in the cytosol and the active GTP-bound form of RhoA is located to the membrane. GDI displacement factors (GDFs) including IκB kinase γ (IKKγ) dissociate the RhoA-GDI complex, allowing activation of RhoA through GEFs. In addition, modifications of Tyr42 phosphorylation and Cys16/20 oxidation in RhoA and Tyr156 phosphorylation and oxidation of RhoGDI promote the dissociation of the RhoA-RhoGDI complex. The expression of RhoA is regulated through transcriptional factors such as c-Myc, HIF-1α/2α, Stat 6, and NF-κB along with several reported microRNAs. As the role of RhoA in regulating actin-filament formation and myosin-actin interaction has been well described, in this review we focus on the transcriptional activity of RhoA and also the regulation of RhoA message itself. Of interest, in the cytosol, activated RhoA induces transcriptional changes through filamentous actin (F-actin)-dependent ("actin switch") or-independent means. RhoA regulates the activity of several transcription regulators such as serum response factor (SRF)/MAL, AP-1, NF-κB, YAP/TAZ, β-catenin, and hypoxia inducible factor (HIF)-1α. Interestingly, RhoA also itself is localized to the nucleus by an as-yet-undiscovered mechanism.

Indexed as

ActinsAnimalsCytosolHumansNF-kappa BrhoA GTP-Binding ProteinTranscription FactorsTranscription, GeneticActinsNF-kappa BrhoA GTP-Binding ProteinTranscription FactorsAP-1MALRhoASRFYAP/TAZβ-catenin

Identifiers

PMID29377108
PMCPMC13482483
OpenAlexW2791645463

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.