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p38γ regulates interaction of nuclear PSF and RNA with the tumour-suppressor hDlg in response to osmotic shock
- Source :
- Journal of Cell Science. 123:2596-2604
- Publication Year :
- 2010
- Publisher :
- The Company of Biologists, 2010.
-
Abstract
- 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.
- Subjects :
- 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
Subjects
Details
- ISSN :
- 14779137 and 00219533
- Volume :
- 123
- Database :
- OpenAIRE
- Journal :
- Journal of Cell Science
- Accession number :
- edsair.doi.dedup.....c0b187877bc83bf3708401ef226e77c2
- Full Text :
- https://doi.org/10.1242/jcs.066514