Modulation of microtubule assembly and stability by phosphatidylinositol action on microtubule-associated protein-2

• Published in: The Journal of biological chemistry Vol. 262; no. 7; pp. 3369 - 3375
• Main Authors: Yamauchi, P.S., Purich, D.L.
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 05.03.1987; American Society for Biochemistry and Molecular Biology
• Subjects: Alkaloids - pharmacology; Animals; Biological and medical sciences; brain; Brain - ultrastructure; Cattle; Cell structures and functions; Cytoskeleton, cytoplasm. Intracellular movements; Fluorescent Antibody Technique; Fundamental and applied biological sciences. Psychology; Glycerol - pharmacology; microtubule-associated protein 2; Microtubule-Associated Proteins - antagonists & inhibitors; Microtubule-Associated Proteins - metabolism; microtubules; Microtubules - drug effects; Microtubules - metabolism; Molecular and cellular biology; Paclitaxel; Phosphatidylinositols - pharmacology; phosphoinositides; Phospholipids - pharmacology; Phosphatidylinositol; Stability; Bovine; Molecular assembly; Animal; Cytoskeleton; Microtubule associated protein; Microtubule

Exposure of elongating (or assembled) bovine brain microtubules to phosphatidylinositol leads to polymerization arrest (or disassembly). The efficiency of phosphatidylinositol far exceeds the action of related phospholipids including phosphatidylethanolamine, phosphatidylcholine, 1,2-diacylglycerol,...