p38γ regulates interaction of nuclear PSF and RNA with the tumour-suppressor hDlg in response to osmotic shock
| Autor: | Paloma del Reino, J. Simon C. Arthur, Maria Isabel Cerezo-Guisado, Ana Cuenda, Francisco Centeno, Francisco Inesta-Vaquera, Guadalupe Sabio, David G. Campbell, Simon Rousseau |
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| Rok vydání: | 2010 |
| Předmět: |
Osmotic shock
RNA-binding protein Plasma protein binding Biology Polymerase Chain Reaction Cell Line Discs Large Homolog 1 Protein Mice Mitogen-Activated Protein Kinase 12 Osmotic Pressure medicine Animals Humans Immunoprecipitation Phosphorylation Kinase activity Nuclear protein PTB-Associated Splicing Factor Cytoskeleton Research Articles Adaptor Proteins Signal Transducing Osmotic concentration Membrane Proteins RNA-Binding Proteins Cell Biology Mice Mutant Strains Cell biology Cell nucleus medicine.anatomical_structure Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization RNA HeLa Cells Protein Binding |
| Zdroj: | Journal of Cell Science. 123:2596-2604 |
| ISSN: | 1477-9137 0021-9533 |
| Popis: | Activation of p38γ modulates the integrity of the complex formed by the human discs large protein (hDlg) with cytoskeletal proteins, which is important for cell adaptation to changes in environmental osmolarity. Here we report that, in response to hyperosmotic stress, p38γ also regulates formation of complexes between hDlg and the nuclear protein polypyrimidine tract-binding protein-associated-splicing factor (PSF). Following osmotic shock, p38γ in the cell nucleus increases its association with nuclear hDlg, thereby causing dissociation of hDlg-PSF complexes. Moreover, hDlg and PSF bind different RNAs; in response to osmotic shock, p38γ causes hDlg-PSF and hDlg-RNA dissociation independently of its kinase activity. These findings identify a novel nuclear complex and suggest a previously unreported function of p38γ, which is independent of its catalytic activity and could affect mRNA processing and/or gene transcription to aid cell adaptation to osmolarity changes in the environment. |
| Databáze: | OpenAIRE |
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