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. (C) 2000 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.