Open Accessp38γ regulates interaction of nuclear PSF and RNA with the tumour-suppressor hDlg in response to osmotic shock
Author(s) -
Guadalupe Sabio,
María Isabel Cerezo-Guisado,
Paloma del Reino,
Francisco Iñesta-Vaquera,
Stéphane Rousseau,
J. Simon C. Arthur,
David G. Campbell,
Francisco Centeno,
Ana Cuenda
Publication year - 2010
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.066514
Subject(s) - biology , microbiology and biotechnology , rna splicing , osmotic shock , transcription factor , alternative splicing , osmotic concentration , rna binding protein , splicing factor , rna , messenger rna , gene , biochemistry
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.