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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Bibliographic Details
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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Summary: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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ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(18)61512-1