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

dc.creatorCambiazo Ayala, Verónica
dc.creatorLogarinho, Elsa
dc.creatorPottstock, Hans
dc.creatorSunkel, Claudio E.
dc.date.accessioned2018-12-20T14:28:48Z
dc.date.available2018-12-20T14:28:48Z
dc.date.created2018-12-20T14:28:48Z
dc.date.issued2000
dc.identifierFEBS Letters, Volumen 483, Issue 1, 2018, Pages 37-42
dc.identifier00145793
dc.identifier10.1016/S0014-5793(00)02077-9
dc.identifierhttp://repositorio.uchile.cl/handle/2250/156146
dc.description.abstractThe 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.
dc.languageen
dc.rightshttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
dc.sourceFEBS Letters
dc.subjectDMAP-85
dc.subjectDrosophila
dc.subjectMicrotubule
dc.subjectMicrotubule-associated protein
dc.subjectMPM-2
dc.subjectPolo kinase
dc.titleMicrotubule binding of the Drosophila DMAP-85 protein is regulated by phosphorylation in vitro
dc.typeArtículos de revistas


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