Tubulin and MAP2 regulate the PCSL phosphatase activity. A possible new role for microtubular proteins.
Eur J Biochem
; 180(1): 15-22, 1989 Mar 01.
Article
em En
| MEDLINE
| ID: mdl-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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Base de dados:
MEDLINE
Assunto principal:
Tubulina (Proteína)
/
4-Nitrofenilfosfatase
/
Monoéster Fosfórico Hidrolases
/
Proteínas Associadas aos Microtúbulos
Limite:
Animals
Idioma:
En
Ano de publicação:
1989
Tipo de documento:
Article