Vimentin serves as a phosphate sink during the apparent activation of protein kinases by okadaic acid in mammalian cells.

The vimentin contents of four mammalian cell lines originating from rat and human tissues were determined by immunoblotting and scanning densitometry. On per cell volume basis, vimentin content in 9L, KD, and HeLa cells was found to be 206.6, 151.6, and 19.1 ng/microliters, respectively. A431 cells were devoid of vimentin. Protein phosphorylation was augmented by treatment of 600 nM okadaic acid for 1 h in these cells. During the apparent activation of protein kinases, vimentin became hyperphosphorylated and the phosphorylation level of other nonvimentin phosphoproteins was relatively little affected in 9L and KD cells. In contrast, cytokeratins and other nonvimentin proteins were heavily phosphorylated in OA-treated HeLa and A431 cells. Regression analysis indicated that the relative increase in phosphorylation level of nonvimentin phosphoproteins was inversely correlated to the contents of vimentin in the four cell lines [r2 = -0.985]. These observations strongly suggest that vimentin acts as a phosphate sink by which the effects of "excess kinase activity" inflicted by phosphatases inhibition was attenuated.