p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP |
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| Authors: | Sabio Guadalupe Arthur James Simon Campbell Kuma Yvonne Peggie Mark Carr Julia Murray-Tait Vicky Centeno Francisco Goedert Michel Morrice Nicholas A Cuenda Ana |
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| Affiliation: | MRC Protein Phosphorylation Unit, University of Dundee, Dundee, UK. |
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| 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 p38gamma MAP kinase (SAPK3/p38gamma) 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/p38gamma-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. |
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