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Fig. 6. Mutation of the two major PKA sites results in a reduction of vimentin phosphorylation and alters the phosphate distribution on vimentin phosphopeptides. When two-dimensional tryptic phosphopeptide mapping of PKA-phosphorylated (A) wild-type and (B) S38:A/S72:A vimentin was performed, peptide 1 showed negligible phosphorylation in the mutant vimentin, whereas peptide 2 showed reduced phosphorylation. Each map was loaded with peptides generated from 5 µg of ³²P-labeled vimentin. The direction of electrophoresis (+,-) and ascending chromatography (arrow) are indicated. (C) An overall reduction in ³²P incorporation as a result of the phosphate-site mutations could be seen when 7.5 µg of wild-type (lane 1) and S38:A/S72:A (lane 2) vimentin, respectively, were phosphorylated in vitro by PKA and subjected to one-dimensional SDS-PAGE followed by autoradiography.

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