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Mars promotes dTACC dephosphorylation on mitotic spindles to ensure spindle stability

By Shengjiang Tan, Ekaterina Lyulcheva, Jon Dean and Daimark Bennett

Abstract

Microtubule-associated proteins (MAPs) ensure the fidelity of chromosome segregation by controlling microtubule (MT) dynamics and mitotic spindle stability. However, many aspects of MAP function and regulation are poorly understood in a developmental context. We show that mars, which encodes a Drosophila melanogaster member of the hepatoma up-regulated protein family of MAPs, is essential for MT stabilization during early embryogenesis. As well as associating with spindle MTs in vivo, Mars binds directly to protein phosphatase 1 (PP1) and coimmunoprecipitates from embryo extracts with minispindles and Drosophila transforming acidic coiled-coil (dTACC), two MAPs that function as spindle assembly factors. Disruption of binding to PP1 or loss of mars function results in elevated levels of phosphorylated dTACC on spindles. A nonphosphorylatable form of dTACC is capable of rescuing the lethality of mars mutants. We propose that Mars mediates spatially controlled dephosphorylation of dTACC, which is critical for spindle stabilization

Topics: Research Articles
Publisher: The Rockefeller University Press
OAI identifier: oai:pubmedcentral.nih.gov:2447907
Provided by: PubMed Central
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    Citations

    1. (2005). Aurora A activates D-TACC – Msps complexes exclusively at centrosomes to stabilize centrosomal microtubules.
    2. (2004). Cloning and expression of mars, a novel member of the guanylate kinase associated protein family
    3. (1993). Sz ö or .
    4. (2006). Towards a comprehensive analysis of the protein phosphatase 1 interactome in Drosophila .

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