ArticlePloS one2020
Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein.
Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 6 citations in OpenAlex.
- A high-resolution data set of fatty acid-binding protein structures. I. Dynamics of FABP4 and ligand binding.Acta crystallographica. Section D, Structural biology · 2025Article
- A high-resolution data set of fatty acid-binding protein structures. II. Crystallographic overview, ligand classes and binding pose.Acta crystallographica. Section D, Structural biology · 2025Article
- Seryl-tRNA Synthetase Shows a Noncanonical Activity of Upregulating Laccase Transcription inMicrobiology spectrum · 2023Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intestinal fatty acid binding protein (FABP) is a small protein expressed along the small intestine that bind long-chain fatty acids and other hydrophobic ligands. Several lines of evidence suggest that, once in the nucleus, it interacts with nuclear receptors, activating them and thus transferring the bound ligand into the nucleus. Previous work by our group suggests that FABP2 would participate in the cytoplasm-nucleus translocation of fatty acids. Because the consensus NLS is absent in the sequence of FABP2, we propose that a 3D signal could be responsible for its nuclear translocation. The results obtained by transfection assays of recombinant wild type and mutated forms of Danio rerio Fabp2 in Caco-2 cell cultures, showed that lysine 17, arginine 29 and lysine 30 residues, which are located in the helix-turn-helix region, would constitute a functional non-classical three-dimensional NLS.
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