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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2005-4-25
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pubmed:abstractText |
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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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-10207622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-10212242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-10329946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-10414979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-10433268,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-10458610,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-10727080,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-10759891,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-10779557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-10856930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-10998351,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-11060025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-11181181,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-11274345,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-11478941,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-11710946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-11865057,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-11909979,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-12141438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-12176742,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-12482988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-12724128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-12766944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-12829478,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-12933808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-14680475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-14699157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-14724236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-14741046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-7891172,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-9024696,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-9115257,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-9368070,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-9430735,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-9512503,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15729360-9742101
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/DLG1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Dlgh1 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase 12,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SAPAP proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
24
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1134-45
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:15729360-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:15729360-Animals,
pubmed-meshheading:15729360-Cell Line, Tumor,
pubmed-meshheading:15729360-Cell Shape,
pubmed-meshheading:15729360-Cell Size,
pubmed-meshheading:15729360-Cytoskeleton,
pubmed-meshheading:15729360-Guanylate Kinase,
pubmed-meshheading:15729360-Humans,
pubmed-meshheading:15729360-Intercellular Junctions,
pubmed-meshheading:15729360-Membrane Proteins,
pubmed-meshheading:15729360-Mice,
pubmed-meshheading:15729360-Mice, Knockout,
pubmed-meshheading:15729360-Mitogen-Activated Protein Kinase 12,
pubmed-meshheading:15729360-Nerve Tissue Proteins,
pubmed-meshheading:15729360-Osmotic Pressure,
pubmed-meshheading:15729360-Phosphorylation,
pubmed-meshheading:15729360-Substrate Specificity
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pubmed:year |
2005
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pubmed:articleTitle |
p38gamma regulates the localisation of SAP97 in the cytoskeleton by modulating its interaction with GKAP.
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pubmed:affiliation |
MRC Protein Phosphorylation Unit, University of Dundee, Dundee, UK.
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