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Article

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

1
Departamento de Biotecnologia, Genética e Biologia Celular, Universidade Estadual de Maringá, Av. Colombo, 5790, Maringá 87020-900, Brazil
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Institut de Recherches Cliniques de Montréal, 110 Avenue des Pins Ouest, Montreal, QC H2W 1R7, Canada
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Departamento de Tecnologia, Campus Umuarama, Universidade Estadual de Maringá, Av. Ângelo Moreira da Fonseca, 1800, Umuarama 87506-370, Brazil
*
Author to whom correspondence should be addressed.
Academic Editor: Hany A. El-Shemy
Curr. Issues Mol. Biol. 2021, 43(2), 767-781; https://doi.org/10.3390/cimb43020056
Received: 30 April 2021 / Revised: 16 June 2021 / Accepted: 24 June 2021 / Published: 22 July 2021
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology Section)
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. View Full-Text
Keywords: KIN (Kin17); cancer biomarker; protein–protein interactions; BioID-MS; splicing process; ribosome biogenesis KIN (Kin17); cancer biomarker; protein–protein interactions; BioID-MS; splicing process; ribosome biogenesis
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MDPI and ACS Style

Gaspar, V.P.; Ramos, A.C.; Cloutier, P.; Pattaro Junior, J.R.; Duarte Junior, F.F.; Bouchard, A.; Seixas, F.A.V.; Coulombe, B.; Fernandez, M.A. Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein. Curr. Issues Mol. Biol. 2021, 43, 767-781. https://doi.org/10.3390/cimb43020056

AMA Style

Gaspar VP, Ramos AC, Cloutier P, Pattaro Junior JR, Duarte Junior FF, Bouchard A, Seixas FAV, Coulombe B, Fernandez MA. Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein. Current Issues in Molecular Biology. 2021; 43(2):767-781. https://doi.org/10.3390/cimb43020056

Chicago/Turabian Style

Gaspar, Vanessa P., Anelise C. Ramos, Philippe Cloutier, José R. Pattaro Junior, Francisco F. Duarte Junior, Annie Bouchard, Flavio A.V. Seixas, Benoit Coulombe, and Maria A. Fernandez 2021. "Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein" Current Issues in Molecular Biology 43, no. 2: 767-781. https://doi.org/10.3390/cimb43020056

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