Modulation of microtubule assembly and stability by phosphatidylinositol action on microtubule-associated protein-2
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,...
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Published in | The Journal of biological chemistry Vol. 262; no. 7; pp. 3369 - 3375 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
Bethesda, MD
Elsevier Inc
05.03.1987
American Society for Biochemistry and Molecular Biology |
Subjects | |
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Abstract | 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, phosphatidylserine, phosphatidylglycerol, or phosphatidic acid. Phosphatidylinositol increases the apparent critical concentration for assembly, and the inhibitory effect of phosphatidylinositol on polymerization is reversed at higher concentrations of microtubule-associated proteins (MAP)s. Taxol- and glycerol-treated microtubules are insensitive to the destabilizing action of phosphatidylinositol; centrifugation and subsequent gel electrophoresis of such samples revealed that both MAP-2a and MAP-2b were selectively desorbed. Likewise, the desorption of MAP-2 was visualized by indirect immunofluorescence microscopy using primary antibodies directed toward tubulin and MAP-2. The instability of microtubules exposed to phosphatidylinositol appears to be related to the MAP-2 content. |
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AbstractList | 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, phosphatidylserine, phosphatidylglycerol, or phosphatidic acid. Phosphatidylinositol increases the apparent critical concentration for assembly, and the inhibitory effect of phosphatidylinositol on polymerization is reversed at higher concentrations of microtubule-associated proteins (MAP)s. Taxol- and glycerol-treated microtubules are insensitive to the destabilizing action of phosphatidylinositol; centrifugation and subsequent gel electrophoresis of such samples revealed that both MAP-2a and MAP-2b were selectively desorbed. Likewise, the desorption of MAP-2 was visualized by indirect immunofluorescence microscopy using primary antibodies directed toward tubulin and MAP-2. The instability of microtubules exposed to phosphatidylinositol appears to be related to the MAP-2 content. 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, phosphatidylserine, phosphatidylglycerol, or phosphatidic acid. Phosphatidylinositol increases the apparent critical concentration for assembly, and the inhibitory effect of phosphatidylinositol on polymerization is reversed at higher concentrations of microtubule-associated proteins (MAP)s. Taxol- and glycerol-treated microtubules are insensitive to the destabilizing action of phosphatidylinositol; centrifugation and subsequent gel electrophoresis of such samples revealed that both MAP-2a and MAP-2b were selectively desorbed. Likewise, the desorption of MAP-2 was visualized by indirect immunofluorescence microscopy using primary antibodies directed toward tubulin and MAP-2. The instability of microtubules exposed to phosphatidylinositol appears to be related to the MAP-2 content. 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, phosphatidylserine, phosphatidylglycerol, or phosphatidic acid. Phosphatidylinositol increases the apparent critical concentration for assembly, and the inhibitory effect of phosphatidylinositol on polymerization is reversed at higher concentrations of microtubule-associated proteins (MAP)s. The instability of microtubules exposed to phosphatidylinositol appears to be related to the MAP-2 content. |
Author | Yamauchi, P.S. Purich, D.L. |
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Keywords | Phosphatidylinositol Stability Bovine Molecular assembly Animal Cytoskeleton Microtubule associated protein Microtubule |
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Snippet | Exposure of elongating (or assembled) bovine brain microtubules to phosphatidylinositol leads to polymerization arrest (or disassembly). The efficiency of... Exposure of elongating (or assembled) bovine brain microtubules to phosphatidylinositol leads to polymerization arrest (or disassembly). The efficiency of... |
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SubjectTerms | 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 |
Title | Modulation of microtubule assembly and stability by phosphatidylinositol action on microtubule-associated protein-2 |
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