Premium
p38γ regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP
Author(s) -
Sabio Guadalupe,
Arthur James Simon Campbell,
Kuma Yvonne,
Peggie Mark,
Carr Julia,
MurrayTait Vicky,
Centeno Francisco,
Goedert Michel,
Morrice Nicholas A,
Cuenda Ana
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600578
Subject(s) - phosphorylation , library science , biology , art history , art , microbiology and biotechnology , computer science
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 p38γ 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.