Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein
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 cellul...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-07-01
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| Series: | Current Issues in Molecular Biology |
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| Online Access: | https://www.mdpi.com/1467-3045/43/2/56 |
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| author | 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 |
| author_facet | 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 |
| author_sort | Vanessa Pinatto Gaspar |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-10T07:47:17Z |
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| institution | Directory Open Access Journal |
| issn | 1467-3037 1467-3045 |
| language | English |
| last_indexed | 2024-03-10T07:47:17Z |
| publishDate | 2021-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Current Issues in Molecular Biology |
| spelling | doaj.art-4addf34c6ecd413b8d574e420f5f23e52023-11-22T12:31:04ZengMDPI AGCurrent Issues in Molecular Biology1467-30371467-30452021-07-0143276778110.3390/cimb43020056Interactome Analysis of KIN (Kin17) Shows New Functions of This ProteinVanessa Pinatto Gaspar0Anelise Cardoso Ramos1Philippe Cloutier2José Renato Pattaro Junior3Francisco Ferreira Duarte Junior4Annie Bouchard5Flavio Augusto Vicente Seixas6Benoit Coulombe7Maria Aparecida Fernandez8Departamento de Biotecnologia, Genética e Biologia Celular, Universidade Estadual de Maringá, Av. Colombo, 5790, Maringá 87020-900, BrazilDepartamento de Biotecnologia, Genética e Biologia Celular, Universidade Estadual de Maringá, Av. Colombo, 5790, Maringá 87020-900, BrazilInstitut de Recherches Cliniques de Montréal, 110 Avenue des Pins Ouest, Montreal, QC H2W 1R7, CanadaDepartamento de Tecnologia, Campus Umuarama, Universidade Estadual de Maringá, Av. Ângelo Moreira da Fonseca, 1800, Umuarama 87506-370, BrazilDepartamento de Biotecnologia, Genética e Biologia Celular, Universidade Estadual de Maringá, Av. Colombo, 5790, Maringá 87020-900, BrazilInstitut de Recherches Cliniques de Montréal, 110 Avenue des Pins Ouest, Montreal, QC H2W 1R7, CanadaDepartamento de Tecnologia, Campus Umuarama, Universidade Estadual de Maringá, Av. Ângelo Moreira da Fonseca, 1800, Umuarama 87506-370, BrazilInstitut de Recherches Cliniques de Montréal, 110 Avenue des Pins Ouest, Montreal, QC H2W 1R7, CanadaDepartamento de Biotecnologia, Genética e Biologia Celular, Universidade Estadual de Maringá, Av. Colombo, 5790, Maringá 87020-900, BrazilKIN (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.https://www.mdpi.com/1467-3045/43/2/56KIN (Kin17)cancer biomarkerprotein–protein interactionsBioID-MSsplicing processribosome biogenesis |
| spellingShingle | 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 Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein Current Issues in Molecular Biology KIN (Kin17) cancer biomarker protein–protein interactions BioID-MS splicing process ribosome biogenesis |
| title | Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein |
| title_full | Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein |
| title_fullStr | Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein |
| title_full_unstemmed | Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein |
| title_short | Interactome Analysis of KIN (Kin17) Shows New Functions of This Protein |
| title_sort | interactome analysis of kin kin17 shows new functions of this protein |
| topic | KIN (Kin17) cancer biomarker protein–protein interactions BioID-MS splicing process ribosome biogenesis |
| url | https://www.mdpi.com/1467-3045/43/2/56 |
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