PUBLICATION
Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein
- Authors
- Suárez, M., Canclini, L., Esteves, A.
- ID
- ZDB-PUB-201120-104
- Date
- 2020
- Source
- PLoS One 15: e0242312 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Protein Binding
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism
- Fatty Acid-Binding Proteins/chemistry
- Fatty Acid-Binding Proteins/genetics
- Fatty Acid-Binding Proteins/metabolism*
- Nuclear Localization Signals/chemistry
- Humans
- Microscopy, Confocal
- Animals
- Mutagenesis
- Amino Acid Sequence
- Cell Nucleus/metabolism*
- Fatty Acids/metabolism
- Zebrafish/metabolism
- Recombinant Proteins/biosynthesis
- Recombinant Proteins/chemistry
- Recombinant Proteins/isolation & purification
- Caco-2 Cells
- Protein Conformation, alpha-Helical
- PubMed
- 33180886 Full text @ PLoS One
Citation
Suárez, M., Canclini, L., Esteves, A. (2020) Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein. PLoS One. 15:e0242312.
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping