Article
- The EMBO Journal (2005) 24, 1134 - 1145
- doi:10.1038/sj.emboj.7600578
Published online: 24 February 2005
Subject Categories:
p38
regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP
Guadalupe Sabio1,3, James Simon Campbell Arthur1, Yvonne Kuma1, Mark Peggie1, Julia Carr1, Vicky Murray-Tait2, Francisco Centeno3, Michel Goedert4, Nicholas A Morrice1 and Ana Cuenda1
- MRC Protein Phosphorylation Unit, University of Dundee, Dundee, UK
- School of Life Sciences, University of Dundee, Dundee, UK
- Departmento Bioquímica y Biología Molecular, Facultad de Veterinaria, Universidad de Extremadura, Cáceres, Spain
- MRC Laboratory of Molecular Biology, Hills Road, Cambridge, UK
Correspondence to:
Ana Cuenda, MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dow St., Dundee DD1 5EH, UK. Tel.: +44 1382 344241; Fax: +44 1382 223778; E-mail: a.i.cuenda@dundee.ac.uk
Received 6 August 2004; Accepted 19 January 2005
Abstract
Activation of the p38 MAP kinase pathways is crucial for the adaptation of mammalian cells to changes in the osmolarity of the environment. Here we identify SAP97/hDlg, the mammalian homologue of the Drosophila tumour suppressor Dlg, as a physiological substrate for the p38
MAP kinase (SAPK3/p38) isoform. SAP97/hDlg is a scaffold protein that forms multiprotein complexes with a variety of proteins and is targeted to the cytoskeleton by its association with the protein guanylate kinase-associated protein (GKAP). The SAPK3/p38-catalysed phosphorylation of SAP97/hDlg triggers its dissociation from GKAP and therefore releases it from the cytoskeleton. This is likely to regulate the integrity of intercellular–junctional complexes, and cell shape and volume in response to osmotic stress.
Keywords:
- knockout,
- osmotic shock,
- PDZ,
- p38,
- stress-activated protein kinase-4/p38
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