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

• Type: Article in International Scientific Journal
• Date: 2000

Authors

Cambiazo, V (Author) Other; Logarinho, E (Author) Other; Pottstock, H (Author) Other; Sunkel, CE (Author) ICBAS

Journal

Title: FEBS Letters

Vol. 483

Pages: 37-42

ISSN: 0014-5793

Publisher: Wiley-Blackwell

Indexing

ISI Web of Knowledge - 8 Citations

Scopus - 9 Citations

Other information

Authenticus ID: P-000-YQS

DOI: 10.1016/s0014-5793(00)02077-9

Abstract (EN): 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6