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. 2003 Feb 18;100(5):2432–2437. doi: 10.1073/pnas.0438011100

Figure 3.

Figure 3

Phosphorylated BimL is released from DLC1. (A and B) Cells were cotransfected with 0.3 μg of epitope-tagged BimL and DLC1 expression vectors together with 0.05 μg of a Bcl2 expression vector. The effect of coexpression of activated JNK1 was investigated. The presence of BimL and DLC1 in the cell lysate was examined by immunoblot (IB) analysis. Coimmunoprecipitation analysis was performed by immunoblot analysis of DLC1 immunoprecipitates (IP) with an antibody to Bim. The results of mutational analysis of the Bim phosphorylation sites Ser-44, Thr-56, and Ser-58 replaced with Asp (A) or with Ala (B) are shown. (C) DLC1 interacts with nonphosphorylated BimL. Cells were cotransfected with 0.3 μg of BimL, 0.05 μg of Bcl2, 0.3 μg of activated JNK1, and 0.5 μg of DLC1 expression vectors. The amount of BimL and DLC1 in cell lysates and in DLC1 immunoprecipitates was examined by immunoblot analysis. Phosphorylated BimL with reduced electrophoretic mobility was not coimmunoprecipitated with DLC1.