The intracellular interplay between galectin-1 and FGF12 in the assembly of ribosome biogenesis complex
Galectin
DOI:
10.1186/s12964-024-01558-1
Publication Date:
2024-03-11T05:01:51Z
AUTHORS (10)
ABSTRACT
Abstract Galectins constitute a class of lectins that specifically interact with β-galactoside sugars in glycoconjugates and are implicated diverse cellular processes, including transport, autophagy or signaling. Since most the activity galectins depends on their ability to bind sugar chains, exert functions mainly extracellular space at cell surface, which microenvironments highly enriched glycoconjugates. also abundant inside cells, but specific intracellular largely unknown. Here we report galectin-1, -3, -7 -8 directly proteinaceous core fibroblast growth factor 12 (FGF12) cytosol nucleus. We demonstrate binding galectin-1 FGF12 blocks secretion. Furthermore, show affects assembly FGF12-containing nuclear/nucleolar ribosome biogenesis complexes consisting NOLC1 TCOF1. Our data provide new link between FGF proteins, revealing an unexpected glycosylation-independent interplay these groups proteins.
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