Tyrosines 113, 128, and 145 of SLP-76 are required for optimal augmentation of NFAT promoter activity
| Autor: | N, Fang, D G, Motto, S E, Ross, G A, Koretzky |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
NFATC Transcription Factors
Gene Expression Regulation Leukemic T-Lymphocytes Molecular Sequence Data Receptors Antigen T-Cell Nuclear Proteins Protein-Tyrosine Kinases Phosphoproteins Neoplasm Proteins DNA-Binding Proteins Structure-Activity Relationship Tumor Cells Cultured Humans Interleukin-2 Leukemia-Lymphoma Adult T-Cell Tyrosine Amino Acid Sequence Phosphorylation Promoter Regions Genetic Protein Processing Post-Translational Adaptor Proteins Signal Transducing Signal Transduction Transcription Factors |
| Zdroj: | Journal of immunology (Baltimore, Md. : 1950). 157(9) |
| ISSN: | 0022-1767 |
| Popis: | SLP-76 (SH2 domain leukocyte protein of 76 kDa) is a recently identified substrate of the TCR-stimulated protein tyrosine kinases that functions in the signal transduction cascade linking the TCR with IL-2 gene expression. In this report, we demonstrate that engagement of the TCR results in tyrosine phosphorylation of SLP-76 in its amino-terminal acidic region. Two tyrosines (Y113 and Y128) fall within an identical five amino-acid motif and are shown to be phosphorylated upon TCR ligation. Although mutation of either Y113 and Y128 has a minimal effect on SLP-76 function, mutation of both residues decreases significantly the ability of SLP-76 to promote T cell activation. A third tyrosine within the amino-terminal region (Y145) appears to be the most important for optimal SLP-76 function, as altering it alone to phenylalanine has a potent impact on SLP-76 augmentation of NFAT promoter activity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|