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p38γ regulates interaction of nuclear PSF and RNA with the tumour-suppressor hDlg in response to osmotic shock

Authors :
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
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.

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