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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Main Authors: Aleksandra Gędaj, Aleksandra Chorążewska, Krzysztof Ciura, Radosław Karelus, Dominika Żukowska, Martyna Biaduń, Marta Kalka, Małgorzata Zakrzewska, Natalia Porębska, Łukasz Opaliński
Format: Article
Language:English
Published: BMC 2024-03-01
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.
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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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