Phosphorylation at threonine-235 by a ras-dependent mitogen-activated protein kinase cascade is essential for transcription factor NF-IL6
| Autor: | Shizuo Akira, Tatsuru Sasagawa, Shigemi Kinoshita, Koichi Sasaki, Tadamitsu Kishimoto, Masanobu Naruto, Toshihiro Nakajima |
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| Rok vydání: | 1993 |
| Předmět: |
Threonine
musculoskeletal diseases Molecular Sequence Data Protein Sorting Signals Transfection Peptide Mapping Mass Spectrometry Mice immune system diseases Animals Protein phosphorylation Amino Acid Sequence Phosphorylation Luciferases Protein kinase A MAPK14 Calcium-Calmodulin-Dependent Protein Kinases Leucine Zippers Binding Sites Multidisciplinary biology Kinase Nuclear Proteins 3T3 Cells Molecular biology biological factors Activating transcription factor 2 DNA-Binding Proteins Genes ras Gene Expression Regulation Mitogen-activated protein kinase CCAAT-Enhancer-Binding Proteins Mutagenesis Site-Directed biology.protein Peptides Protein Kinases Transcription Factors Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 90:2207-2211 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.90.6.2207 |
| Popis: | NF-IL6, a member of the basic leucine zipper (bZIP) family transcription factors, is involved in expression of inducible genes involved in immune and inflammatory responses. We observed that coexpression of oncogenic p21ras stimulated the transactivating activity of NF-IL6 and induced phosphorylation of Thr-235 located just N-terminal to the DNA binding domain of NF-IL6. Recently, mitogen-activated protein (MAP) kinases have been shown to be implicated in the cellular response to activated ras. Purified MAP kinases specifically phosphorylated Thr-235 of NF-IL6 in vitro. Mutation of Thr-235 abolished the ras-dependent activation of NF-IL6. From these results, we conclude that NF-IL6 is regulated through phosphorylation by MAP kinases in response to activated ras. |
| Databáze: | OpenAIRE |
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