Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation.

Abstract excerpt

Mutation of the major site of in vivo tyrosine phosphorylation of p56lck (tyrosine 505) to a phenylalanine constitutively enhances the p56lck-associated tyrosine-specific protein kinase activity. The mutant polypeptide is extensively phosphorylated in vivo at the site of in vitro Lck autophosphorylation (tyrosine 394) and is capable of oncogenic transformation of rodent fibroblasts. These observations have...

Topics

• Animals
• Base Sequence
• Cell Compartmentation
• Cell Line
• Cell Membrane
• DNA
• DNA Mutational Analysis
• Enzyme Activation
• Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
• Lymphocytes
• Mice