Evidence map›Paper›PMID 34449532›Full record

ArticleCurrent issues in molecular biology2021

Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein.

Vanessa Pinatto Gaspar, Anelise Cardoso Ramos, Philippe Cloutier, José Renato Pattaro Junior, Francisco Ferreira Duarte Junior, Annie Bouchard, Flavio Augusto Vicente Seixas, Benoit Coulombe, Maria Aparecida Fernandez

Open access · goldAbstract read
In one paragraph

Article in Current issues in molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.6field-weighted citation impact, top 36% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

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  5. Review
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 2 institutions in 2 countries.

Vanessa Pinatto GasparDepartamento de Biotecnologia, Genética e Biologia Celular, Universidade Estadual de Maringá, Av. Colombo, 5790, Maringá 87020-900, Brazil.ORCID 0000-0001-6800-0857
Anelise Cardoso RamosDepartamento de Biotecnologia, Genética e Biologia Celular, Universidade Estadual de Maringá, Av. Colombo, 5790, Maringá 87020-900, Brazil.ORCID 0000-0003-4387-3832
Philippe CloutierInstitut de Recherches Cliniques de Montréal, 110 Avenue des Pins Ouest, Montreal, QC H2W 1R7, Canada.
José Renato Pattaro JuniorDepartamento de Tecnologia, Campus Umuarama, Universidade Estadual de Maringá, Av. Ângelo Moreira da Fonseca, 1800, Umuarama 87506-370, Brazil.ORCID 0000-0002-3904-3919
Francisco Ferreira Duarte JuniorDepartamento de Biotecnologia, Genética e Biologia Celular, Universidade Estadual de Maringá, Av. Colombo, 5790, Maringá 87020-900, Brazil.ORCID 0000-0002-7494-2848
Annie BouchardInstitut de Recherches Cliniques de Montréal, 110 Avenue des Pins Ouest, Montreal, QC H2W 1R7, Canada.
Flavio Augusto Vicente SeixasDepartamento de Tecnologia, Campus Umuarama, Universidade Estadual de Maringá, Av. Ângelo Moreira da Fonseca, 1800, Umuarama 87506-370, Brazil.ORCID 0000-0002-0117-6919
Benoit CoulombeInstitut de Recherches Cliniques de Montréal, 110 Avenue des Pins Ouest, Montreal, QC H2W 1R7, Canada.
Maria Aparecida FernandezDepartamento de Biotecnologia, Genética e Biologia Celular, Universidade Estadual de Maringá, Av. Colombo, 5790, Maringá 87020-900, Brazil.ORCID 0000-0002-7696-5680
Universidade Estadual de Maringá · BRMontreal Clinical Research Institute · CA

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 204994/2014-4Conselho Nacional de Desenvolvimento Científico e Tecnológico 305960/2015-6Fundação Araucária 40/16Fundação Araucária 53/19
6 · The paper itself

Abstract

KIN (Kin17) protein is overexpressed in a number of cancerous cell lines, and is therefore considered a possible cancer biomarker. It is a well-conserved protein across eukaryotes and is ubiquitously expressed in all cell types studied, suggesting an important role in the maintenance of basic cellular function which is yet to be well determined. Early studies on KIN suggested that this nuclear protein plays a role in cellular mechanisms such as DNA replication and/or repair; however, its association with chromatin depends on its methylation state. In order to provide a better understanding of the cellular role of this protein, we investigated its interactome by proximity-dependent biotin identification coupled to mass spectrometry (BioID-MS), used for identification of protein-protein interactions. Our analyses detected interaction with a novel set of proteins and reinforced previous observations linking KIN to factors involved in RNA processing, notably pre-mRNA splicing and ribosome biogenesis. However, little evidence supports that this protein is directly coupled to DNA replication and/or repair processes, as previously suggested. Furthermore, a novel interaction was observed with PRMT7 (protein arginine methyltransferase 7) and we demonstrated that KIN is modified by this enzyme. This interactome analysis indicates that KIN is associated with several cell metabolism functions, and shows for the first time an association with ribosome biogenesis, suggesting that KIN is likely a moonlight protein.

Indexed as

Cells, CulturedChromatinDNA-Binding ProteinsHumansNeoplasmsNuclear ProteinsProtein-Arginine N-MethyltransferasesProtein Interaction MapsRibosomesRNA-Binding ProteinsRNA SplicingChromatinDNA-Binding ProteinsKIN protein, humanNuclear ProteinsPRMT7 protein, humanProtein-Arginine N-MethyltransferasesRNA-Binding ProteinsBioID-MScancer biomarkerKIN (Kin17)protein–protein interactionsribosome biogenesissplicing process

Identifiers

PMID34449532
PMCPMC8929021
OpenAlexW3184019802

What OpenQuestion holds

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LicenceCC BY
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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.