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. 2017 Apr 15;28(8):1147–1159. doi: 10.1091/mbc.E16-09-0632

FIGURE 8:

FIGURE 8:

Lyn mutated in the SH2 or SH3 domain or in the palmitoylation site enhances phosphorylation of p38 and prevents its nuclear translocation in RAW264 cells. Cells expressing indicated constructs of Lyn-GFP or GFP alone as a control were stimulated with 100 ng/ml LPS for 30 min. (A) Cell lysates were analyzed for the presence of phospho-p38 (p-p38) by immunoblotting and densitometry. Histogram shows mean ± SD from three experiments. The values of p38 phosphorylation were normalized against p38 content in samples and are expressed relative to those in cells transfected with GFP alone. *Significantly different from LPS-stimulated cells transfected with GFP alone at p ≤ 0.05. (B, C) Cytoplasmic and nuclear proteins were analyzed for the presence of p-p38, actin, or histone H3. Results of one experiment representative of two to four.