Microtubule binding of the Drosophila DMAP-85 protein is regulated by phosphorylation in vitro

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Abstract

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. Copyright (C) 2000 Federation of European Biochemical Societies.

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Cambiazo, V., Logarinho, E., Pottstock, H., & Sunkel, C. E. (2000). Microtubule binding of the Drosophila DMAP-85 protein is regulated by phosphorylation in vitro. FEBS Letters, 483(1), 37–42. https://doi.org/10.1016/S0014-5793(00)02077-9

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