p38 gamma regulates interaction of nuclear PSF and RNA with the tumour-suppressor hDlg in response to osmotic shock. / Sabio, Guadalupe; Cerezo-Guisado, Maria I.; del Reino, Paloma; Inesta-Vaquera, Francisco A.; Rousseau, Simon; Arthur, J. Simon C.; Campbell, David G.; Centeno, Francisco; Cuenda, Ana.
In: Journal of Cell Science, Vol. 123, No. 15, 01.08.2010, p. 2596-2604.Research output: Contribution to journal › Article
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TY - JOUR
T1 - p38 gamma regulates interaction of nuclear PSF and RNA with the tumour-suppressor hDlg in response to osmotic shock
A1 - Sabio,Guadalupe
A1 - Cerezo-Guisado,Maria I.
A1 - del Reino,Paloma
A1 - Inesta-Vaquera,Francisco A.
A1 - Rousseau,Simon
A1 - Arthur,J. Simon C.
A1 - Campbell,David G.
A1 - Centeno,Francisco
A1 - Cuenda,Ana
AU - Sabio,Guadalupe
AU - Cerezo-Guisado,Maria I.
AU - del Reino,Paloma
AU - Inesta-Vaquera,Francisco A.
AU - Rousseau,Simon
AU - Arthur,J. Simon C.
AU - Campbell,David G.
AU - Centeno,Francisco
AU - Cuenda,Ana
PY - 2010/8/1
Y1 - 2010/8/1
N2 - <p>Activation of p38 gamma 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, p38 gamma also regulates formation of complexes between hDlg and the nuclear protein polypyrimidine tract-binding protein-associated-splicing factor (PSF). Following osmotic shock, p38 gamma 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, p38 gamma 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 p38 gamma, 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.</p>
AB - <p>Activation of p38 gamma 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, p38 gamma also regulates formation of complexes between hDlg and the nuclear protein polypyrimidine tract-binding protein-associated-splicing factor (PSF). Following osmotic shock, p38 gamma 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, p38 gamma 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 p38 gamma, 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.</p>
U2 - 10.1242/jcs.066514
DO - 10.1242/jcs.066514
M1 - Article
JO - Journal of Cell Science
JF - Journal of Cell Science
SN - 0021-9533
IS - 15
VL - 123
SP - 2596
EP - 2604
ER -