Open AccessTubulin and MAP2 regulate the PCS L phosphatase activite
Author(s) -
JESSUS Catherine,
GPROS Jozef,
CAYLA Xavier,
HERMANN Jacques,
HENDRIX Peter,
OZON René,
MERLEVEDE Wilfried
Publication year - 1989
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1989.tb14609.x
Subject(s) - phosphatase , computer science , microbiology and biotechnology , biology , phosphorylation
Tubulin can stimulate specifically the aryl phosphatase activity of the low‐ M r polycation‐stimulated (PCS L ) 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 (A 50 = 60 nM) and is due to an increase in V max . 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 elimiate this inhibitory effect. MAP2 also inhibits the polycation‐stimulated phosphorylase phosphatase activity.