| Abstract: |
Palmitylation of Src family tyrosine kinases has been shown to play a role in directing their membrane localization. Here we demonstrate that palmitylation can also regulate recognition and tyrosine phosphorylation of the B cell Src kinase substrate Igα. Blk and Src, which are not palmitylated, phosphorylate co-expressed Igα in Cos cells, whereas palmitylated Src kinases do not. Addition of a palmitylation site to Blk abrogates its phosphorylation of the substrate, while mutation of Fyn's palmitylation sites results in recognition and phosphorylation of Igα. These results indicate that palmitylation, a reversible protein modification, aids in regulating recognition of physiologic substrates by Src family tyrosine kinases. |
| Keywords: |
signal transduction; controlled study; protein phosphorylation; proto-oncogene proteins; nonhuman; animal cell; animals; immunoglobulin; transfection; protein tyrosine kinase; structure activity relation; cos cells; phosphorylation; b lymphocyte; animalia; b-lymphocytes; amino acid sequence; recombinant fusion proteins; substrate specificity; mutagenesis, site-directed; antigens, cd; src-family kinases; enzyme structure; enzyme modification; palmitoylation; receptors, antigen, b-cell; proto-oncogene proteins c-fyn; palmitic acids; priority journal; article; antigens, cd79
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