Microtubule binding of the drosophila DMAP-85 protein is regulated by phosphorylation in vitro.
The phosphorylation of microtubule-associated proteins (MAPs) is thought to be a key factor in the regulation of microtubule (MT) stability. Previously we isolated DMAP-85, a Drosophila MAP shown to be associated with stable MTs. In this work we show that DMAP-85 phosphorylated in cell-free early embryo extracts is released from MTs. MPM-2 antibodies recognize the phosphorylated protein. In vitro, DMAP-85 can be phosphorylated by the mitotic kinase Polo affecting its binding to MTs and creating MPM-2 epitopes on the protein. The results suggest that phosphorylation of DMAP-85 might affect its MT stabilizing activity during early mitotic cycles.
Cambiazo
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Laboratorio de Biologia Celular, INTa, Universidad de Chile, Macul 5540 Santiago, Chile. vcambiaz@uec.inta.uchile.cl
Logarinho
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Pottstock
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Sunkel
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D000818:Animals; D000911:Antibodies, Monoclonal / Q000378:metabolism; D004330:Drosophila / Q000737:chemistry / Q000196:embryology; D029721:Drosophila Proteins; D000939:Epitopes / Q000378:metabolism; D052998:Microcystins; D008869:Microtubule-Associated Proteins / Q000235:genetics / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism*; D010456:Peptides, Cyclic / Q000494:pharmacology; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism
D000911:Antibodies, Monoclonal; D029721:Drosophila Proteins; D000939:Epitopes; D052998:Microcystins; D008869:Microtubule-Associated Proteins; D010456:Peptides, Cyclic; D010750:Phosphoproteins; D011994:Recombinant Proteins; C078588:microcystin; C072004:polo protein, Drosophila; D017346:Protein Serine-Threonine Kinases