LiCl inhibits phosphorylation of β-catenin but not cyclin D1: NIH3T3 cells were cultured in medium containing 25 mM LiCl (columns 3, 4), 50 mM LiCl (column 5), or control medium with NaCl (columns 1, 2). In some cultures MG132 was added to block degradation of phosphorylated proteins (columns 2, 3, 5; see legend at the top). After 4 hrs lysates were prepared and probed for β-catenin, β-catenin phosphorylated on Ser 33/37/Thr 41, cyclin D1, cyclin D1 phosphorylated on Thr-286, and for actin as a loading control. (A) Photographs of the western results are presented. Each band was then quantitated, and (B) the ratio of phosphorylated cyclin D1 divided by the level of total cyclin D1 protein was determined and plotted immediately below the corresponding western bands. In addition, (C) the ratio of phosphorylated β-catenin divided by the level of total β-catenin protein is presented. Quantitative results correspond to the bands displayed in this figure immediately above them (with the same lane numbers).
Yang et al. BMC Cell Biology 2006 7:33 doi:10.1186/1471-2121-7-33