p38γ regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP

Guadalupe Sabio, James Simon Campbell Arthur, Yvonne Kuma, Mark Peggie, Julia Carr, Vicky Murray-Tait, Francisco Centeno, Michel Goedert, Nicholas A. Morrice, Ana Cuenda (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    202 Citations (Scopus)

    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 p38aγ MAP kinase (SAPK3/p38γ) 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/p38γ-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.

    Original languageEnglish
    Pages (from-to)1134-1145
    Number of pages12
    JournalEMBO Journal
    Volume24
    Issue number6
    DOIs
    Publication statusPublished - 23 Mar 2005

    Keywords

    • Knockout
    • Osmotic shock
    • p38γ
    • PDZ
    • Stress-activated protein kinase-4/p38δ

    ASJC Scopus subject areas

    • General Neuroscience
    • Molecular Biology
    • General Biochemistry,Genetics and Molecular Biology
    • General Immunology and Microbiology

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