Identification of tyrosine 620 as the major phosphorylation site of myelin-associated glycoprotein and its implication in interacting with signaling molecules
| Autor: | John C. Bell, Daniel E. H. Afar, M. L. Jaramillo, G. Almazan |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
biology
Tyrosine phosphorylation Cell Biology Protein tyrosine phosphatase SH2 domain environment and public health Biochemistry FLT4 Receptor tyrosine kinase enzymes and coenzymes (carbohydrates) chemistry.chemical_compound nervous system chemistry biology.protein Phosphorylation Tyrosine Molecular Biology Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Journal of Biological Chemistry. 269:27240-27245 |
| ISSN: | 0021-9258 |
| Popis: | Myelin-associated glycoprotein (MAG) is a myelin-specific cell adhesion molecule of the immunoglobulin supergene family and is tyrosine-phosphorylated in the developing brain. To define the role of MAG in signal transduction, the tyrosine phosphorylation sites were analyzed. The major tyrosine phosphorylation residue was identified as Tyr-620, which was found to interact specifically with the SH2 domains of phospholipase C (PLC gamma). This domain may represent a novel protein binding motif that can be regulated by tyrosine phosphorylation. MAG also specifically bound the Fyn tyrosine kinase, suggesting that MAG serves as a docking protein that allows the interaction between different signaling molecules. |
| Databáze: | OpenAIRE |
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