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. 2014 Feb 25;9(2):e89604. doi: 10.1371/journal.pone.0089604

Figure 1. In vitro interaction of the SH3 domain of Fyn kinase with the proline-rich domain of LKB1 (A) Purified His-LKB1-WT fusion protein was immobilized onto cobalt beads and incubated either with purified GST protein (control), GST-Fyn-WT or GST-Fyn-W119A fusion protein.

Figure 1

Retained proteins were separated onto SDS-polyacrylamide gel electrophoresis. Binding was detected using anti-GST (detecting Fyn kinase) and anti-His (detecting LKB1) antibodies. Blots are representative of 4 independent experiments. (B) Purified His-LKB1-WT or His-LKB1-P328A mutant fusion protein was immobilized onto cobalt beads and incubated with either purified GST protein (control) or GST-Fyn-WT. Binding was detected using anti-GST (detecting Fyn kinase) and anti-His (detecting LKB1) antibodies. (C) Purified His-LKB1-WT or His-LKB1-P328A mutant were incubated with GST-Fyn-kinase for the indicated time. Phosphorylation of LKB1 was detected by the phospho-tyrosine specific 4G10 antibody. Blots are representative of 3 independent experiments. D. Signal quantification. Identical letters indicate values that are not statistically different from each other (P>0.05).