Tubulin and MAP2 regulate the PCSL phosphatase activite

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Abstract
Tubulin can stimulate specifically the aryl phosphatase activity of the low-M1 polycation-stimulated (PCSL) phosphatase, measured as p-nitrophenyl phosphatase activity, or using reduced carboxamidomethylated and maleylated (RCM) lysozyme, phosphorylated on tyrosyl residues, as a substrate. This stimulation is independent of the degree of polymerization of tubulin (A50 = 60 nM) and is due to an increase in Vmax. It is mechanistically different from the ATP-induced activation and resistant to heat and trypsin treatment. Chymotrypsin destroys the stimulatory effect of tubulin. The polycation-stimulated phosphorylase phosphatase activity is inhibited by tubulin, probably by a polycation/polyanion interaction. The microtubule-associated protein, MAP2, is inhibitory to the p-nitrophenyl phosphatase activity and tubulin can eliminate this inhibitory effect. MAP2 also inhibits the polycation-stimulated phosphorylase phosphatase activity.