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Fig. 1. MARCKS expression and its phosphorylation in myoblasts. (A) Representative northern blot showing the expression of MARCKS transcript in myoblasts in culture. The expression in brain was used as a positive control. 18S ribosomal RNA was used for a loading control. (B) Western blot analysis showing the expression of MARCKS protein in myoblasts in culture. Brain protein was used as a positive control. (C) Western blot analysis showing MARCKS distribution between membrane pellet (P) and cytosolic (C) compartments at various time points after plating cells on fibronectin (FN). (D) Western blot analysis of phosphorylated MARCKS in myoblasts as a function of time after plating myoblasts on fibronectin. The expression of MARCKS protein did not show any significant changes over the same time course. (E) In vivo phosphorylation labeling of MARCKS. Myoblasts were labeled with [³²P]-orthophosphate after plating on fibronectin. Phosphorylated MARCKS was immunoprecipitated at indicated times after plating and run on SDS-PAGE as described in Materials and Methods. The amount of MARCKS immunoprecipitated is shown after probing the blot with an anti-MARCKS polyclonal antibody. Studies were done in the absence or presence of the PKC inhibitor, calphostin C, as indicated. (F) Phosphorylation of MARCKS in control myoblasts (GFP vector alone) and in myoblasts overexpressing PKC-GFP. MARCKS phosphorylation is shown by western blot analysis at different time points after the cells were plated on fibronectin.

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