Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein
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
| 2020 | |
|
Fatty Acid-Binding Proteins Protein binding Recombinant proteins Cell Nucleus Nuclear localization signals Zebrafish proteins |
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| Inglés | |
| Universidad de la República | |
| COLIBRI | |
| https://hdl.handle.net/20.500.12008/31777 | |
| Acceso abierto | |
| Licencia Creative Commons Atribución (CC - By 4.0) |
| _version_ | 1807522789971722240 |
|---|---|
| author | Suárez Martins, Mariana Carolina |
| author2 | Canclini, Lucía Esteves, Adriana |
| author2_role | author author |
| author_facet | Suárez Martins, Mariana Carolina Canclini, Lucía Esteves, Adriana |
| author_role | author |
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| collection | COLIBRI |
| dc.contributor.filiacion.none.fl_str_mv | Suárez Martins Mariana Carolina, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología. Canclini Lucía, IIBCE Esteves Adriana, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología. |
| dc.creator.editor.none.fl_str_mv | Witt, S. N. |
| dc.creator.none.fl_str_mv | Suárez Martins, Mariana Carolina Canclini, Lucía Esteves, Adriana |
| dc.date.accessioned.none.fl_str_mv | 2022-06-01T13:39:07Z |
| dc.date.available.none.fl_str_mv | 2022-06-01T13:39:07Z |
| dc.date.issued.none.fl_str_mv | 2020 |
| dc.description.abstract.none.fl_txt_mv | 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 |
| dc.format.extent.es.fl_str_mv | 14 h. |
| dc.format.mimetype.es.fl_str_mv | application/pdf |
| dc.identifier.citation.es.fl_str_mv | Suárez, M, Canclini, L y Esteves, A. "Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein". PLoS ONE. [en línea] 2020, 15(11): e0242312. 14 h. DOI: 10.1371/journal.pone.0242312 |
| dc.identifier.doi.none.fl_str_mv | 10.1371/journal.pone.0242312 |
| dc.identifier.issn.none.fl_str_mv | 1932-6203 |
| dc.identifier.uri.none.fl_str_mv | https://hdl.handle.net/20.500.12008/31777 |
| dc.language.iso.none.fl_str_mv | en eng |
| dc.publisher.en.fl_str_mv | Public Library of Science |
| dc.relation.ispartof.es.fl_str_mv | PLoS ONE, 2020, 15(11): e0242312 |
| dc.rights.license.none.fl_str_mv | Licencia Creative Commons Atribución (CC - By 4.0) |
| dc.rights.none.fl_str_mv | info:eu-repo/semantics/openAccess |
| dc.source.none.fl_str_mv | reponame:COLIBRI instname:Universidad de la República instacron:Universidad de la República |
| dc.subject.en.fl_str_mv | Fatty Acid-Binding Proteins Protein binding Recombinant proteins Cell Nucleus Nuclear localization signals Zebrafish proteins |
| dc.title.none.fl_str_mv | Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein |
| dc.type.es.fl_str_mv | Artículo |
| dc.type.none.fl_str_mv | info:eu-repo/semantics/article |
| dc.type.version.none.fl_str_mv | info:eu-repo/semantics/publishedVersion |
| description | 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 |
| eu_rights_str_mv | openAccess |
| format | article |
| id | COLIBRI_206de37c92b1e6ce91075742e227d077 |
| identifier_str_mv | Suárez, M, Canclini, L y Esteves, A. "Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein". PLoS ONE. [en línea] 2020, 15(11): e0242312. 14 h. DOI: 10.1371/journal.pone.0242312 1932-6203 10.1371/journal.pone.0242312 |
| instacron_str | Universidad de la República |
| institution | Universidad de la República |
| instname_str | Universidad de la República |
| language | eng |
| language_invalid_str_mv | en |
| network_acronym_str | COLIBRI |
| network_name_str | COLIBRI |
| oai_identifier_str | oai:colibri.udelar.edu.uy:20.500.12008/31777 |
| publishDate | 2020 |
| reponame_str | COLIBRI |
| repository.mail.fl_str_mv | mabel.seroubian@seciu.edu.uy |
| repository.name.fl_str_mv | COLIBRI - Universidad de la República |
| repository_id_str | 4771 |
| rights_invalid_str_mv | Licencia Creative Commons Atribución (CC - By 4.0) |
| spelling | Suárez Martins Mariana Carolina, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.Canclini Lucía, IIBCEEsteves Adriana, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.2022-06-01T13:39:07Z2022-06-01T13:39:07Z2020Suárez, M, Canclini, L y Esteves, A. "Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein". PLoS ONE. [en línea] 2020, 15(11): e0242312. 14 h. DOI: 10.1371/journal.pone.02423121932-6203https://hdl.handle.net/20.500.12008/3177710.1371/journal.pone.0242312The 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 NLSSubmitted by Verdun Juan Pablo (jverdun@fcien.edu.uy) on 2022-05-30T22:51:33Z No. of bitstreams: 2 license_rdf: 19875 bytes, checksum: 9fdbed07f52437945402c4e70fa4773e (MD5) 10.1371journal.pone.0242312.pdf: 1607091 bytes, checksum: d48fc699114025f612afeabe41b15fcc (MD5)Approved for entry into archive by Faget Cecilia (lfaget@fcien.edu.uy) on 2022-06-01T12:55:01Z (GMT) No. of bitstreams: 2 license_rdf: 19875 bytes, checksum: 9fdbed07f52437945402c4e70fa4773e (MD5) 10.1371journal.pone.0242312.pdf: 1607091 bytes, checksum: d48fc699114025f612afeabe41b15fcc (MD5)Made available in DSpace by Luna Fabiana (fabiana.luna@seciu.edu.uy) on 2022-06-01T13:39:07Z (GMT). No. of bitstreams: 2 license_rdf: 19875 bytes, checksum: 9fdbed07f52437945402c4e70fa4773e (MD5) 10.1371journal.pone.0242312.pdf: 1607091 bytes, checksum: d48fc699114025f612afeabe41b15fcc (MD5) Previous issue date: 202014 h.application/pdfenengPublic Library of SciencePLoS ONE, 2020, 15(11): e0242312Las obras depositadas en el Repositorio se rigen por la Ordenanza de los Derechos de la Propiedad Intelectual de la Universidad de la República.(Res. Nº 91 de C.D.C. de 8/III/1994 – D.O. 7/IV/1994) y por la Ordenanza del Repositorio Abierto de la Universidad de la República (Res. Nº 16 de C.D.C. de 07/10/2014)info:eu-repo/semantics/openAccessLicencia Creative Commons Atribución (CC - By 4.0)Fatty Acid-Binding ProteinsProtein bindingRecombinant proteinsCell NucleusNuclear localization signalsZebrafish proteinsIdentification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding proteinArtículoinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionreponame:COLIBRIinstname:Universidad de la Repúblicainstacron:Universidad de la RepúblicaSuárez Martins, Mariana CarolinaCanclini, LucíaEsteves, AdrianaWitt, S. 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- Universidad de la Repúblicafalse |
| spellingShingle | Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein Suárez Martins, Mariana Carolina Fatty Acid-Binding Proteins Protein binding Recombinant proteins Cell Nucleus Nuclear localization signals Zebrafish proteins |
| status_str | publishedVersion |
| title | Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein |
| title_full | Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein |
| title_fullStr | Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein |
| title_full_unstemmed | Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein |
| title_short | Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein |
| title_sort | Identification of a non-classical three-dimensional nuclear localization signal in the intestinal fatty acid binding protein |
| topic | Fatty Acid-Binding Proteins Protein binding Recombinant proteins Cell Nucleus Nuclear localization signals Zebrafish proteins |
| url | https://hdl.handle.net/20.500.12008/31777 |
