dc.creator | Baños Jaime, Blanca | es |
dc.creator | Corrales Guerrero, Laura | es |
dc.creator | Pérez Mejías, Gonzalo | es |
dc.creator | Rejano Gordillo, Claudia M. | es |
dc.creator | Velázquez Campoy, Adrián | es |
dc.creator | Martínez Cruz, Luis Alfonso | es |
dc.creator | Rosa Acosta, Miguel Ángel de la | es |
dc.creator | Díaz Moreno, Irene | es |
dc.date.accessioned | 2024-07-17T12:09:08Z | |
dc.date.available | 2024-07-17T12:09:08Z | |
dc.date.issued | 2024-07-05 | |
dc.identifier.citation | Baños Jaime, B., Corrales Guerrero, L., Pérez Mejías, G., Rejano Gordillo, C.M., Velázquez Campoy, A., Martínez Cruz, L.A.,...,Díaz Moreno, I. (2024). Phosphorylation at the disordered N-end makes HuR accumulate and dimerize in the cytoplasm.. Nucleic Acids Research, 2024, gkae564. https://doi.org/10.1093/nar/gkae564. | |
dc.identifier.issn | 0305-1048 | es |
dc.identifier.issn | 1362-4962 | es |
dc.identifier.uri | https://hdl.handle.net/11441/161484 | |
dc.description.abstract | Human antigen R (HuR) is an RNA binding protein mainly involved in maintaining the stability and controlling the translation of mRNAs, critical
for immune response, cell survival, proliferation and apoptosis. Although HuR is a nuclear protein, its mRNA translational-related function occurs
at the cytoplasm, where the oligomeric form of HuR is more abundant. However, the regulation of nucleo-cytoplasmic transport of HuR and
its connection with protein oligomerization remain unclear. In this work, we describe the phosphorylation of Tyr5 as a new hallmark for HuR
activation. Our biophysical, structural and computational assays using phosphorylated and phosphomimetic HuR proteins demonstrate that
phosphorylation of Tyr5 at the disordered N-end stretch induces global changes on HuR dynamics and conformation, modifying the solvent
accessible surface of the HuR nucleo-cytoplasmic shuttling (HNS) sequence and releasing regions implicated in HuR dimerization. These findings
explain the preferential cytoplasmic accumulation of phosphorylated HuR in HeLa cells, aiding to comprehend the mechanisms underlying HuR
nucleus-cytoplasm shuttling and its later dimerization, both of which are relevant in HuR-related pathogenesis. | es |
dc.description.sponsorship | Agencia Estatal de Investigación española (AEI), el Ministerio de Ciencia e Innovación de España (MCIN) y 'FEDER Una forma de hacer Europa' - PID2021-126663NB-I00 y PID2020-117116RP | es |
dc.description.sponsorship | Junta de Andalucía - P18-FR-3487 y PAIDI-Doctor 2020 DOC_00796 | es |
dc.description.sponsorship | Ministerio de Educación, Cultura y Deporte de España - FPU17/04604 | es |
dc.format | application/pdf | es |
dc.format.extent | 14 p. | es |
dc.language.iso | eng | es |
dc.publisher | Oxford University Press | es |
dc.relation.ispartof | Nucleic Acids Research, 2024, gkae564. | |
dc.rights | Atribución-NoComercial 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc/4.0/ | * |
dc.title | Phosphorylation at the disordered N-end makes HuR accumulate and dimerize in the cytoplasm. | es |
dc.type | info:eu-repo/semantics/article | es |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular | es |
dc.relation.publisherversion | https://doi.org/10.1093/nar/gkae564 | es |
dc.identifier.doi | 10.1093/nar/gkae564 | es |
dc.journaltitle | Nucleic Acids Research | es |
dc.publication.volumen | 2024 | es |
dc.publication.initialPage | gkae564 | es |
dc.contributor.funder | Agencia Estatal de Investigación. España | es |
dc.contributor.funder | Ministerio de Ciencia e Innovación (MICIN). España | es |
dc.contributor.funder | European Commission (EC). Fondo Europeo de Desarrollo Regional (FEDER) | es |
dc.contributor.funder | Junta de Andalucía | es |
dc.contributor.funder | Universidad de Sevilla | es |
dc.contributor.funder | Ministerio de Educación, Cultura y Deporte (MECD). España | es |