The intracellular interplay between galectin-1 and FGF12 in the assembly of ribosome biogenesis complex
Abstract Galectins constitute a class of lectins that specifically interact with β-galactoside sugars in glycoconjugates and are implicated in diverse cellular processes, including transport, autophagy or signaling. Since most of the activity of galectins depends on their ability to bind sugar chain...
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BMC
2024-03-01
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Series: | Cell Communication and Signaling |
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Online Access: | https://doi.org/10.1186/s12964-024-01558-1 |
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author | Aleksandra Gędaj Aleksandra Chorążewska Krzysztof Ciura Radosław Karelus Dominika Żukowska Martyna Biaduń Marta Kalka Małgorzata Zakrzewska Natalia Porębska Łukasz Opaliński |
author_facet | Aleksandra Gędaj Aleksandra Chorążewska Krzysztof Ciura Radosław Karelus Dominika Żukowska Martyna Biaduń Marta Kalka Małgorzata Zakrzewska Natalia Porębska Łukasz Opaliński |
author_sort | Aleksandra Gędaj |
collection | DOAJ |
description | Abstract Galectins constitute a class of lectins that specifically interact with β-galactoside sugars in glycoconjugates and are implicated in diverse cellular processes, including transport, autophagy or signaling. Since most of the activity of galectins depends on their ability to bind sugar chains, galectins exert their functions mainly in the extracellular space or at the cell surface, which are microenvironments highly enriched in glycoconjugates. Galectins are also abundant inside cells, but their specific intracellular functions are largely unknown. Here we report that galectin-1, -3, -7 and -8 directly interact with the proteinaceous core of fibroblast growth factor 12 (FGF12) in the cytosol and in nucleus. We demonstrate that binding of galectin-1 to FGF12 in the cytosol blocks FGF12 secretion. Furthermore, we show that intracellular galectin-1 affects the assembly of FGF12-containing nuclear/nucleolar ribosome biogenesis complexes consisting of NOLC1 and TCOF1. Our data provide a new link between galectins and FGF proteins, revealing an unexpected glycosylation-independent intracellular interplay between these groups of proteins. |
first_indexed | 2024-04-24T23:04:57Z |
format | Article |
id | doaj.art-7abc2bf200b245dd85ac1e7aedaaa749 |
institution | Directory Open Access Journal |
issn | 1478-811X |
language | English |
last_indexed | 2024-04-24T23:04:57Z |
publishDate | 2024-03-01 |
publisher | BMC |
record_format | Article |
series | Cell Communication and Signaling |
spelling | doaj.art-7abc2bf200b245dd85ac1e7aedaaa7492024-03-17T12:33:05ZengBMCCell Communication and Signaling1478-811X2024-03-012211910.1186/s12964-024-01558-1The intracellular interplay between galectin-1 and FGF12 in the assembly of ribosome biogenesis complexAleksandra Gędaj0Aleksandra Chorążewska1Krzysztof Ciura2Radosław Karelus3Dominika Żukowska4Martyna Biaduń5Marta Kalka6Małgorzata Zakrzewska7Natalia Porębska8Łukasz Opaliński9Department 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 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 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 Engineering, Faculty of Biotechnology, University of WroclawAbstract Galectins constitute a class of lectins that specifically interact with β-galactoside sugars in glycoconjugates and are implicated in diverse cellular processes, including transport, autophagy or signaling. Since most of the activity of galectins depends on their ability to bind sugar chains, galectins exert their functions mainly in the extracellular space or at the cell surface, which are microenvironments highly enriched in glycoconjugates. Galectins are also abundant inside cells, but their specific intracellular functions are largely unknown. Here we report that galectin-1, -3, -7 and -8 directly interact with the proteinaceous core of fibroblast growth factor 12 (FGF12) in the cytosol and in nucleus. We demonstrate that binding of galectin-1 to FGF12 in the cytosol blocks FGF12 secretion. Furthermore, we show that intracellular galectin-1 affects the assembly of FGF12-containing nuclear/nucleolar ribosome biogenesis complexes consisting of NOLC1 and TCOF1. Our data provide a new link between galectins and FGF proteins, revealing an unexpected glycosylation-independent intracellular interplay between these groups of proteins.https://doi.org/10.1186/s12964-024-01558-1FHFFGF12GalectinsSecretionNucleolusNOLC1 |
spellingShingle | Aleksandra Gędaj Aleksandra Chorążewska Krzysztof Ciura Radosław Karelus Dominika Żukowska Martyna Biaduń Marta Kalka Małgorzata Zakrzewska Natalia Porębska Łukasz Opaliński The intracellular interplay between galectin-1 and FGF12 in the assembly of ribosome biogenesis complex Cell Communication and Signaling FHF FGF12 Galectins Secretion Nucleolus NOLC1 |
title | The intracellular interplay between galectin-1 and FGF12 in the assembly of ribosome biogenesis complex |
title_full | The intracellular interplay between galectin-1 and FGF12 in the assembly of ribosome biogenesis complex |
title_fullStr | The intracellular interplay between galectin-1 and FGF12 in the assembly of ribosome biogenesis complex |
title_full_unstemmed | The intracellular interplay between galectin-1 and FGF12 in the assembly of ribosome biogenesis complex |
title_short | The intracellular interplay between galectin-1 and FGF12 in the assembly of ribosome biogenesis complex |
title_sort | intracellular interplay between galectin 1 and fgf12 in the assembly of ribosome biogenesis complex |
topic | FHF FGF12 Galectins Secretion Nucleolus NOLC1 |
url | https://doi.org/10.1186/s12964-024-01558-1 |
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