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 inThe Journal of biological chemistry Vol. 262; no. 7; pp. 3369 - 3375
Main Authors Yamauchi, P.S., Purich, D.L.
Format Journal Article
LanguageEnglish
Published Bethesda, MD Elsevier Inc 05.03.1987
American Society for Biochemistry and Molecular Biology
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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.
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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Issue 7
Keywords Phosphatidylinositol
Stability
Bovine
Molecular assembly
Animal
Cytoskeleton
Microtubule associated protein
Microtubule
Language English
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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
URI https://dx.doi.org/10.1016/S0021-9258(18)61512-1
http://www.jbc.org/content/262/7/3369.abstract
https://www.ncbi.nlm.nih.gov/pubmed/2880849
https://search.proquest.com/docview/14597152
https://search.proquest.com/docview/77395069
Volume 262
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