Article
The unique amino-terminal domain of p56lck regulates interactions with tyrosine protein phosphatases in T lymphocytes.
Molecular and cellular biology - 1 May 1995
Gervais F G, Veillette A
Abstract excerpt
The catalytic activity of p56lck is repressed by phosphorylation of a conserved carboxy-terminal tyrosine residue (tyrosine 505). Accumulating data show that this phosphorylation is mediated by the tyrosine protein kinase p50csk and that it is reversed by the transmembrane tyrosine protein phosph...
Topics
- 3T3 Cells
- Amino Acid Sequence
- Animals
- Base Sequence
- Binding Sites
- Cell Line
- DNA Primers
- Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
- Mice
- Molecular Sequence Data
- Mutation
- Phosphorylation