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

Cambiazo, V; Logarinho, E; Pottstock, H; Sunkel, CE

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.

Más información

Título según WOS: Microtubule binding of the Drosophila DMAP-85 protein is regulated by phosphorylation in vitro
Título según SCOPUS: Microtubule binding of the Drosophila DMAP-85 protein is regulated by phosphorylation in vitro
Título de la Revista: FEBS LETTERS
Volumen: 483
Número: 1
Editorial: Wiley
Fecha de publicación: 2000
Página de inicio: 37
Página final: 42
Idioma: English
URL: http://linkinghub.elsevier.com/retrieve/pii/S0014579300020779
DOI:

10.1016/S0014-5793(00)02077-9

Notas: ISI, SCOPUS