Evidence map›Paper›PMID 28623334›Full record

ArticleScientific reports2017

Novel complex of HAT protein TIP60 and nuclear receptor PXR promotes cell migration and adhesion.

Karishma Bakshi, B Ranjitha, Shraddha Dubey, Jaisri Jagannadham, Bharti Jaiswal, Ashish Gupta

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

17 citing papers in PubMed, 29 citations in OpenAlex.

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  14. PXR: a center of transcriptional regulation in cancer.Acta pharmaceutica Sinica. B · 2020
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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

6 authors at 1 institution in 1 country.

Karishma BakshiDepartment of Life Sciences, Shiv Nadar University, Greater Noida, India.
B RanjithaDepartment of Life Sciences, Shiv Nadar University, Greater Noida, India.
Shraddha DubeyDepartment of Life Sciences, Shiv Nadar University, Greater Noida, India.
Jaisri JagannadhamDepartment of Life Sciences, Shiv Nadar University, Greater Noida, India.
Bharti JaiswalDepartment of Life Sciences, Shiv Nadar University, Greater Noida, India.
Ashish GuptaDepartment of Life Sciences, Shiv Nadar University, Greater Noida, India. ag315@snu.edu.in.
Shiv Nadar University · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PXR is a member of nuclear receptor superfamily and a well-characterized mediator of xenobiotic metabolism. The classical mode of PXR activation involves its binding to appropriate ligand and subsequent heterodimerization with its partner RXR. However, various factors such as post-translational modifications and crosstalk with different cellular factors may also regulate the functional dynamics and behavior of PXR. In the present study, we have identified that TIP60, an essential lysine acetyltransferase protein interacts with unliganded PXR and together this complex promotes cell migration & adhesion. TIP60 utilizes its NR Box to interact with LBD region of PXR and acetylates PXR at lysine 170 to induce its intranuclear reorganization. Also, RXR is not required for TIP60-PXR complex formation and this complex does not induce ligand-dependent PXR target gene transactivation. Interestingly, we observed that PXR augments the catalytic activity of TIP60 for histones. This is the first report demonstrating the exclusive interaction of TIP60 with PXR and uncovers a potential role for the TIP60-PXR complex in cell migration and adhesion.

Indexed as

Cell AdhesionCell MovementAcetylationCatalysisCell NucleusHumansLigandsLysine Acetyltransferase 5Models, BiologicalModels, MolecularProtein BindingProtein ConformationProtein Interaction Domains and MotifsReceptors, Cytoplasmic and NuclearStructure-Activity RelationshipKAT5 protein, humanLigandsLysine Acetyltransferase 5Receptors, Cytoplasmic and Nuclear

Identifiers

PMID28623334
PMCPMC5473911
OpenAlexW2622537992

What OpenQuestion holds

Textmetadata
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.