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pubmed-article:9865614pubmed:abstractTextPhosphorylation, dimerization and binding to calmodulin have been reported to influence the microtubule assembly capacities of MAPs (microtubule-associated proteins). Here we report that the Drosophila 205K MAP is a phosphoprotein in vivo and can be phosphorylated by cdc2/p34 in vitro. Bacterially produced 205K MAP is competent of microtubule assembly and microtubule bundling and binds to immobilized calmodulin in a Ca2+-dependent way. EM rotary shadowing analyses suggest that 205K MAP consists of an amino-terminal flexible extended region and a carboxy-terminal globular domain. This carboxy-terminal region harbors the microtubule binding site and sequences required for dimerization, as confirmed by in vitro crosslinking experiments of truncated proteins.lld:pubmed
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pubmed-article:9865614pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:9865614pubmed:year1998lld:pubmed
pubmed-article:9865614pubmed:articleTitleAnalysis of structure and microtubule assembly activity of the Drosophila 205K MAP.lld:pubmed
pubmed-article:9865614pubmed:affiliationDivision of Oncology, University of Geneva Medical Center, Switzerland.lld:pubmed
pubmed-article:9865614pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9865614pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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