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Published online July 14, 2008
doi:10.1083/jcb.200712080
The Journal of Cell Biology, Vol. 182, No. 1, 27-33
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Tan et al.
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Mars promotes dTACC dephosphorylation on mitotic spindles to ensure spindle stability

Shengjiang Tan1,2, Ekaterina Lyulcheva1,2, Jon Dean1, and Daimark Bennett1,2

1 Department of Zoology, Oxford University, Oxford OX1 3PS, England, UK
2 School of Biological Sciences, Biosciences Building, University of Liverpool, Liverpool L69 7ZB, England, UK

Correspondence to Daimark Bennett: daimark.bennett{at}liverpool.ac.uk

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.

Abbreviations used in this paper: dTACC, Drosophila transforming acidic coiled coil; FM, FLAG-Myc; HURP, hepatoma up-regulated protein; MAP, microtubule-associated protein; Msps, minispindles; MT, microtubule; p-dTACC; phosphorylated dTACC; PP1, protein phosphatase 1.


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