Article
Interleukin-2 induces tyrosine phosphorylation of the vav proto-oncogene product in human T cells: lack of requirement for the tyrosine kinase lck.
The Biochemical journal - 1 Sept 1993
Evans G A, Howard O M, Erwin R, Farrar W L
Abstract excerpt
The haematopoietic protein, p95vav, has been shown to be a tyrosine kinase substrate and to have tyrosine kinase-modulated guanine-nucleotide-releasing-factor activity. This implies a function in the control of ras or ras-like proteins. Because ras activation has been shown to be a downstream eve...
Topics
- Cell Cycle Proteins
- Humans
- Immunoblotting
- Immunosorbent Techniques
- Interleukin-2
- Lymphocyte Activation
- Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
- Lymphoma
- Mutation
- Phosphotyrosine
- Phytohemagglutinins
- Protein-Tyrosine Kinases
- Proto-Oncogene Mas
- Proto-Oncogene Proteins
- Proto-Oncogene Proteins c-vav
- Signal Transduction
- T-Lymphocytes
- Tumor Cells, Cultured