English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/95798
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Citado 8 veces en Web of Knowledge®  |  Pub MebCentral Ver citas en PubMed Central  |  Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar EndNote (RIS)Exportar EndNote (RIS)
Título

HuR thermal stability is dependent on domain binding and upon phosphorylation

Autor Scheiba, Rafael M.; Aroca, Ángeles ; Díaz-Moreno, Irene
Palabras clave RNA Binding Protein
Post-translational Modifications
RNA Recognition Motif
Protein Thermal Stability
Phosphorylation
HuR
Fecha de publicación 2012
EditorSpringer
Citación European Biophysics Journal 41: 597- 605 (2012)
ResumenHuman antigen R (HuR) is a multitasking RNA binding protein involved in posttranscriptional regulation by recognizing adenine- and uracile-rich elements placed at the 3′-untranslated regions of messenger RNAs (mRNAs). The modular architecture of the protein, which consists of two N-terminal RNA recognition motifs (RRMs) in tandem spaced from a third one by a nuclear-cytoplasmic shuttling sequence, controls the stability of many mRNA targets, as well as their translation rates. A higher level of regulation comes from the fact that both localization and function of HuR are strictly regulated by phosphorylation. Here, we report how the thermal stability of RRM2 is decreased by the presence of RRM1, indicating that both domains are interacting in solution. In addition, even though no significant structural changes are observed among mutants of HuR RRM12 mimicking phosphorylated species, slight differences in stability are appreciable, which may explain the RNA binding activity of HuR. © European Biophysical Societies' Association 2012.
URI http://hdl.handle.net/10261/95798
DOI10.1007/s00249-012-0827-3
Identificadoresdoi: 10.1007/s00249-012-0827-3
issn: 0175-7571
Aparece en las colecciones: (IBVF) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
EBJO-D-11-00227 - Digital CSIC.pdf438,23 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 



NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.