Three domains of SLP-76 are required for its optimal function in a T cell line
Autor: | M A Musci, D G Motto, S E Ross, N Fang, G A Koretzky |
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Rok vydání: | 1997 |
Předmět: | |
Zdroj: | The Journal of Immunology. 159:1639-1647 |
ISSN: | 1550-6606 0022-1767 |
DOI: | 10.4049/jimmunol.159.4.1639 |
Popis: | We and others have shown that overexpression of SLP-76 augments TCR-stimulated IL-2 promoter activity in the Jurkat T cell line. In this report we investigate the signaling mechanisms through which SLP-76 mediates its effect on T cell activation. We show that overexpressed SLP-76 acts downstream of TCR-stimulated protein tyrosine kinases, but does not affect calcium signaling. Overexpression of SLP-76 does, however, augment TCR stimulation of both ERK (extracellular signal-regulated kinase) activity and a reporter construct driven by activating protein-1 binding sites. Structure/function analysis reveals that three distinct regions of SLP-76, each important for protein associations, are required for augmentation of TCR-induced nuclear factor-AT activity. These data suggest that SLP-76 functions as an adapter molecule that requires three unique domains to link proximal TCR signals in T cells. |
Databáze: | OpenAIRE |
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