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  • Title: Tubulin and MAP2 regulate the PCSL phosphatase activity. A possible new role for microtubular proteins.
    Author: Jessus C, Goris J, Cayla X, Hermann J, Hendrix P, Ozon R, Merlevede W.
    Journal: Eur J Biochem; 1989 Mar 01; 180(1):15-22. PubMed ID: 2540001.
    Abstract:
    Tubulin can stimulate specifically the aryl phosphatase activity of the low-Mr 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.
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