FGF12 is a novel component of the nucleolar NOLC1/TCOF1 ribosome biogenesis complex
Abstract Among the FGF proteins, the least characterized superfamily is the group of fibroblast growth factor homologous factors (FHFs). To date, the main role of FHFs has been primarily seen in the modulation of voltage-gated ion channels, but a full picture of the function of FHFs inside the cell...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2022-11-01
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| Series: | Cell Communication and Signaling |
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| Online Access: | https://doi.org/10.1186/s12964-022-01000-4 |
| _version_ | 1811187092646002688 |
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| author | Martyna Sochacka Radoslaw Karelus Lukasz Opalinski Daniel Krowarsch Martyna Biadun Jacek Otlewski Malgorzata Zakrzewska |
| author_facet | Martyna Sochacka Radoslaw Karelus Lukasz Opalinski Daniel Krowarsch Martyna Biadun Jacek Otlewski Malgorzata Zakrzewska |
| author_sort | Martyna Sochacka |
| collection | DOAJ |
| description | Abstract Among the FGF proteins, the least characterized superfamily is the group of fibroblast growth factor homologous factors (FHFs). To date, the main role of FHFs has been primarily seen in the modulation of voltage-gated ion channels, but a full picture of the function of FHFs inside the cell is far from complete. In the present study, we focused on identifying novel FGF12 binding partners to indicate its intracellular functions. Among the identified proteins, a significant number were nuclear proteins, especially RNA-binding proteins involved in translational processes, such as ribosomal processing and modification. We have demonstrated that FGF12 is localized to the nucleolus, where it interacts with NOLC1 and TCOF1, proteins involved in the assembly of functional ribosomes. Interactions with both NOLC1 and TCOF1 are unique to FGF12, as other FHF proteins only bind to TCOF1. The formation of nucleolar FGF12 complexes with NOLC1 and TCOF1 is phosphorylation-dependent and requires the C-terminal region of FGF12. Surprisingly, NOLC1 and TCOF1 are unable to interact with each other in the absence of FGF12. Taken together, our data link FHF proteins to nucleoli for the first time and suggest a novel and unexpected role for FGF12 in ribosome biogenesis. Video Abstract |
| first_indexed | 2024-04-11T13:56:11Z |
| format | Article |
| id | doaj.art-a81e8c554fe84a4d83928deb13e1dbef |
| institution | Directory Open Access Journal |
| issn | 1478-811X |
| language | English |
| last_indexed | 2024-04-11T13:56:11Z |
| publishDate | 2022-11-01 |
| publisher | BMC |
| record_format | Article |
| series | Cell Communication and Signaling |
| spelling | doaj.art-a81e8c554fe84a4d83928deb13e1dbef2022-12-22T04:20:20ZengBMCCell Communication and Signaling1478-811X2022-11-0120111410.1186/s12964-022-01000-4FGF12 is a novel component of the nucleolar NOLC1/TCOF1 ribosome biogenesis complexMartyna Sochacka0Radoslaw Karelus1Lukasz Opalinski2Daniel Krowarsch3Martyna Biadun4Jacek Otlewski5Malgorzata Zakrzewska6Department of Protein Engineering, Faculty of Biotechnology, University of WroclawDepartment of Protein Engineering, Faculty of Biotechnology, University of WroclawDepartment of Protein Engineering, Faculty of Biotechnology, University of WroclawDepartment of Protein Biotechnology, Faculty of Biotechnology, University of WroclawDepartment of Protein Engineering, Faculty of Biotechnology, University of WroclawDepartment of Protein Engineering, Faculty of Biotechnology, University of WroclawDepartment of Protein Engineering, Faculty of Biotechnology, University of WroclawAbstract Among the FGF proteins, the least characterized superfamily is the group of fibroblast growth factor homologous factors (FHFs). To date, the main role of FHFs has been primarily seen in the modulation of voltage-gated ion channels, but a full picture of the function of FHFs inside the cell is far from complete. In the present study, we focused on identifying novel FGF12 binding partners to indicate its intracellular functions. Among the identified proteins, a significant number were nuclear proteins, especially RNA-binding proteins involved in translational processes, such as ribosomal processing and modification. We have demonstrated that FGF12 is localized to the nucleolus, where it interacts with NOLC1 and TCOF1, proteins involved in the assembly of functional ribosomes. Interactions with both NOLC1 and TCOF1 are unique to FGF12, as other FHF proteins only bind to TCOF1. The formation of nucleolar FGF12 complexes with NOLC1 and TCOF1 is phosphorylation-dependent and requires the C-terminal region of FGF12. Surprisingly, NOLC1 and TCOF1 are unable to interact with each other in the absence of FGF12. Taken together, our data link FHF proteins to nucleoli for the first time and suggest a novel and unexpected role for FGF12 in ribosome biogenesis. Video Abstracthttps://doi.org/10.1186/s12964-022-01000-4FGF12Protein-protein interactionNucleolusRibosome biogenesisNOLC1TCOF1 |
| spellingShingle | Martyna Sochacka Radoslaw Karelus Lukasz Opalinski Daniel Krowarsch Martyna Biadun Jacek Otlewski Malgorzata Zakrzewska FGF12 is a novel component of the nucleolar NOLC1/TCOF1 ribosome biogenesis complex Cell Communication and Signaling FGF12 Protein-protein interaction Nucleolus Ribosome biogenesis NOLC1 TCOF1 |
| title | FGF12 is a novel component of the nucleolar NOLC1/TCOF1 ribosome biogenesis complex |
| title_full | FGF12 is a novel component of the nucleolar NOLC1/TCOF1 ribosome biogenesis complex |
| title_fullStr | FGF12 is a novel component of the nucleolar NOLC1/TCOF1 ribosome biogenesis complex |
| title_full_unstemmed | FGF12 is a novel component of the nucleolar NOLC1/TCOF1 ribosome biogenesis complex |
| title_short | FGF12 is a novel component of the nucleolar NOLC1/TCOF1 ribosome biogenesis complex |
| title_sort | fgf12 is a novel component of the nucleolar nolc1 tcof1 ribosome biogenesis complex |
| topic | FGF12 Protein-protein interaction Nucleolus Ribosome biogenesis NOLC1 TCOF1 |
| url | https://doi.org/10.1186/s12964-022-01000-4 |
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