Abstract
Proteins coimmunoprecipitating with protein kinase C (PKC) ε in fibroblasts were identified through matrix-assisted laser desorption/ionisation time of flight mass spectrometry (MALDI TOF m/s). This method identified myosin IIA in PKC ε immunoprecipitates, as well as known PKC ε binding proteins, actin, β'Cop and cytokeratin. Myosin is not a substrate for PKC ε. Immunofluorescence analysis showed that PKC ε is colocalised with actin and myosin in actomyosin stress fibers in fibroblasts. Inhibitors of PKC and myosin ATPase activity, as well as microfilament-disrupting drugs, all inhibited spreading of fibroblasts after passage, suggesting a role for a PKC ε–actin–myosin complex in cell spreading.
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