Identification of a phosphorylation site in c-Ski as serine 515
| Autor: | Masao Saitoh, Kazunobu Isogaya, Kohei Miyazono, Motoko Nagata, Shinji Nagata, Keiji Miyazawa, Keiko Yuki |
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| Rok vydání: | 2010 |
| Předmět: |
inorganic chemicals
animal structures Molecular Sequence Data Mutant Biology Biochemistry DNA-binding protein Cell Line Phosphorylation cascade Serine Transforming Growth Factor beta Proto-Oncogene Proteins Animals Humans Protein phosphorylation Amino Acid Sequence Phosphorylation RNA Small Interfering Molecular Biology Gel electrophoresis General Medicine musculoskeletal system DNA-Binding Proteins enzymes and coenzymes (carbohydrates) Signal transduction human activities Signal Transduction |
| Zdroj: | Journal of Biochemistry. |
| ISSN: | 0021-924X |
| DOI: | 10.1093/jb/mvq076 |
| Popis: | c-Ski has been known to be phosphorylated at serine residue(s), which results in slower migration of c-Ski in SDS-polyacrylamide gel electrophoresis. The position(s) of phosphorylation, however, has not been determined. In the present study, we identified a phosphorylation site of c-Ski which affects its electrophoretic motility as serine 515 using MALDI-TOF mass spectrometry. A phosphorylation-resistant mutant, c-Ski S515A, did not exhibit a phosphatase-sensitive band shift. In addition, we confirmed that endogenous c-Ski is phosphorylated at serine 515, using a specific antibody. The phosphorylation status of c-Ski, however, does not appear to affect its stability or effects on TGF-β signalling. Identification of the phosphorylation site of c-Ski would allow us further examination of physiological significance of c-Ski phosphorylation. |
| Databáze: | OpenAIRE |
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