Scaffold protein Dlgh1 coordinates alternative p38 kinase activation, directing T cell receptor signals toward NFAT but not NF-κB transcription factors View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2006-12-24

AUTHORS

June L Round, Lisa A Humphries, Tamar Tomassian, Paul Mittelstadt, Min Zhang, M Carrie Miceli

ABSTRACT

Tyrosine kinases couple the T cell receptor (TCR) to discrete signaling cascades, each of which is capable of inducing a distinct functional outcome. Precisely how TCR signals are channeled toward specific targets remains unclear. TCR stimulation triggers 'alternative' activation of the mitogen-activated protein kinase p38, whereby the Lck and Zap70 tyrosine kinases directly activate p38. Here we report that alternatively activated p38 associated with the Dlgh1 MAGUK scaffold protein. 'Knockdown' of Dlgh1 expression blocked TCR-induced activation of p38 and the transcription factor NFAT but not of the mitogen-activated protein kinase Jnk or transcription factor NF-κB. A Dlgh1 mutant incapable of binding p38 failed to activate NFAT. Along with reports that the CARMA1 MAGUK scaffold protein coordinates activation of Jnk and NF-κB but not of p38 or NFAT, our findings identify MAGUK scaffold proteins as 'orchestrators' of TCR signal specificity. More... »

PAGES

154-161

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ni1422

DOI

http://dx.doi.org/10.1038/ni1422

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1027703121

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/17187070


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