Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein

Suárez Martins, Mariana Carolina - Canclini, Lucía - Esteves, Adriana

Editor(es): Witt, S. N.

Resumen:

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


Detalles Bibliográficos
2020
Fatty Acid-Binding Proteins
Protein binding
Recombinant proteins
Cell Nucleus
Nuclear localization signals
Zebrafish proteins
Inglés
Universidad de la República
COLIBRI
https://hdl.handle.net/20.500.12008/31777
Acceso abierto
Licencia Creative Commons Atribución (CC - By 4.0)