HuR thermal stability is dependent on domain binding and upon phosphorylation
Human 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 reco...
| Autores: | , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión enviada para evaluación y publicación |
| Fecha de publicación: | 2012 |
| País: | España |
| Institución: | Universidad de Sevilla (US) |
| Repositorio: | idUS. Depósito de Investigación de la Universidad de Sevilla |
| OAI Identifier: | oai:idus.us.es:11441/70833 |
| Acceso en línea: | https://hdl.handle.net/11441/70833 https://doi.org/10.1007/s00249-012-0827-3 |
| Access Level: | acceso abierto |
| Palabra clave: | RNA Binding Protein Post-translational Modifications RNA Recognition Motif Protein Thermal Stability Phosphorylation HuR |
| Sumario: | Human 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. |
|---|